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Information on EC 1.2.1.44 - cinnamoyl-CoA reductase
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EC Tree
1.2.1.44 cinnamoyl-CoA reductaseIUBMB Comments
Acts also on a number of substituted cinnamoyl esters of coenzyme A.
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Word Map
- 1.2.1.44
- lignin
-
cinnamyl
- monolignols
-
phenylpropanoids
-
lignification
- xylem
- caffeoyl-coa
- p-coumaroyl-coa
- leucocephala
- ccoaomt
- leucaena
-
4-coumarate:coa
- gunnii
-
sinapoyl
-
guaiacyl
-
syringyl
-
cinnamyl-alcohol
- coniferaldehyde
- sinapoyl-coa
-
lignin-specific
- sinapaldehyde
-
non-condensed
-
thioacidolysis
- biotechnology
- synthesis
- industry
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cinnamoyl-coa reductase, cinnamoyl coa reductase, ll-ccrh1, bpccr1, cinnamoyl-coa reductase 1, ta-ccr2, sbccr1, atccr1, osccr1, sbccr2-2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CCR
CCR1
CCR2
CCRH1
cinnamoyl CoA reductase
cinnamoyl CoA reductase 1
cinnamoyl-CoA reductase
cinnamoyl-CoA reductase 1
cinnamoyl-CoA reductase1
cinnamoyl-CoA:NADPH reductase
-
-
-
-
cinnamoyl-coenzyme A reductase
feruloyl coenzyme A reductase
-
-
-
-
feruloyl-CoA reductase
-
-
-
-
ferulyl-CoA reductase
-
-
-
-
HcCCR1
p-hydroxycinnamoyl coenzyme A reductase
-
-
-
-
reductase, cinnamoyl coenzyme A
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-
-
-
cinnamoyl-coenzyme A reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
also acts on a number of substituted cinnamoyl esters of coenzyme A
-
-
-
cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
although SbCCR1 displays higher affinity for caffeoyl-CoA or 4-coumaroyl-CoA than for feruloyl-CoA, the enzyme shows significantly higher activity for the latter substrate. In the first catalytic step, pro-R hydride transfer occurs from the C4 atom of NADPH to the reactive thioester carbonyl. The resulting oxyanion is temporarily stabilized by the oxyanion hole established from the side chain hydroxyl groups of Ser149 and Tyr183. Collapse of the tetrahedral intermediate is then followed by C-S bond cleavage and protonation of the CoA thiolate, in the presence of NADP+, there is very low affinity for the CoA ester compounds, which precludes the formation of a nonproductive complex, catalytic mechanism and substrate specificity, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating)
Acts also on a number of substituted cinnamoyl esters of coenzyme A.
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CAS REGISTRY NUMBER
COMMENTARY
59929-39-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
-
-
-
?
coumaroyl-CoA + NADPH + H+
coumaraldehyde + CoA + NADP+
activity assay
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
low activity
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
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-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
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low activity
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
i.e. 4,5-dihydroxy-3-methoxycinnamoyl-CoA
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
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i.e. 4,5-dihydroxy-3-methoxycinnamoyl-CoA
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?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
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-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
-
poor substrate
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
low activity
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
low activity
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
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-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
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-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
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-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
activity assay
-
-
?
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
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-
-
r
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
preferenced substrate
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-
r
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
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-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
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-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
low activity
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
catalyzes preferentially the formation of cinnamaldehyde
catalyzes preferentially the formation of cinnamaldehyde
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly preferred substrate
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-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
most favoured substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
preferred substrate for isoform CCR1
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-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate for isozyme CCR1
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-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly specific for
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate of isoform CCR1
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
activity assay
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate, which indicates preferential biosynthesis of G-type lignin
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
-
-
?
p-coumaroyl-CoA + NADPH + H+
p-coumaraldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
low activity
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
very low efficiency
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
preferred substrate of isoform CCR2-1
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
activity assay
-
-
?
additional information
?
-
enzymatic assays with aGST-FaCCR reaction containing a mixture of equal molar amounts of three substrates (caffeoyl-, 4-coumaroyl-, and feruloyl-CoA), yield three major peaks that are identified as caffeic aldehyde (3,4-dihydroxycinnamaldehyde), 4-coumaraldehyde, and coniferaldehyde, respectively
-
-
?
additional information
?
-
-
enzymatic assays with aGST-FaCCR reaction containing a mixture of equal molar amounts of three substrates (caffeoyl-, 4-coumaroyl-, and feruloyl-CoA), yield three major peaks that are identified as caffeic aldehyde (3,4-dihydroxycinnamaldehyde), 4-coumaraldehyde, and coniferaldehyde, respectively
-
-
?
additional information
?
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-
isozyme CCR1 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
isozyme CCR1 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
-
isozyme CCR2 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
isozyme CCR2 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
Ph-CCR1 is most active with feruloyl-CoA, followed by sinapoyl-CoA and 4-coumaroyl-CoA (relative to feruloyl-CoA, 65.4 and 21.6% activity, respectively), and only sparingly active with caffeoyl-CoA and benzoyl-CoA (below 1% activity). Ph-CCR1 exhibits the greatest catalytic efficiency (kcat/Km) with feruloyl-CoA and sinapoyl-CoA
-
-
?
additional information
?
-
-
Ph-CCR1 is most active with feruloyl-CoA, followed by sinapoyl-CoA and 4-coumaroyl-CoA (relative to feruloyl-CoA, 65.4 and 21.6% activity, respectively), and only sparingly active with caffeoyl-CoA and benzoyl-CoA (below 1% activity). Ph-CCR1 exhibits the greatest catalytic efficiency (kcat/Km) with feruloyl-CoA and sinapoyl-CoA
-
-
?
additional information
?
-
CCR converts hydroxycinnamoyl-CoA thioesters to their corresponding cinnamaldehydes in the presence of NADPH
-
-
?
additional information
?
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
no activity with sinapoyl-CoA by chimeric 4CL1-CCR fusion enzyme
-
-
?
additional information
?
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
the substrates of CCR, cinnamoyl-CoA esters, are products of 4-coumarate-CoA ligase (4CL, EC 6.2.1.12), which is an enzyme upstream of CCR. Recombinant Pt4CL can catalyze the conversion of hydroxycinnamic acids to cinnamoyl-CoA esters, with high efficiency
-
-
?
additional information
?
-
although SbCCR1 displays higher affinity for caffeoyl-CoA or 4-coumaroyl-CoA than for feruloyl-CoA, the enzyme shows significantly higher activity for the latter substrate. Substrate specificity, molecular docking, overview. Thr154 of SbCCR1 and other CCRs likely confers strong substrate specificity for feruloyl-CoA over other cinnamoyl-CoA thioesters
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
most favoured substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
preferred substrate for isoform CCR1
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly specific for
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
very low efficiency
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
CCR converts hydroxycinnamoyl-CoA thioesters to their corresponding cinnamaldehydes in the presence of NADPH
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
binding structure analysis. Structural comparisons of the NADP+-complexed form of Ph-CCR1 with the apo forms of both Ph-CCR1 and Medicago trunculata Mt-CCR2 reveals a number of adjustments that are localized to polypeptide chain segments surrounding the central cleft and are undoubtedly a direct consequence of NADP+ binding
NADP+
binding structure analysis. Structural comparisons of the NADP+-complexed form of Ph-CCR1 with the apo forms of both Ph-CCR1 and Medicago trunculata Mt-CCR2 reveals a number of adjustments that are localized to polypeptide chain segments surrounding the central cleft and are undoubtedly a direct consequence of NADP+ binding
NADPH
the conserved motifs G-X-X-G-X-X-A and D-X-X-D are reported to be involved in NAD(P) binding and adenine binding pocket stabilization. In addition, the NADP specificity motif R(X)5K is identified, which is a key structure that distinguishes CCR from other NAD(H)-dependent SDRs
NADPH
the enzyme contains a conserved NAD(P) binding domain VTGAGGFIASWMVKLLLEKGY
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
citraconic anhydride
31% residual activity at 1.5 mM with feruloyl-CoA as substrate
diethylpyrocarbonate
44% residual activity at 3 mM with feruloyl-CoA as substrate
N-acetyl imidazole
50% residual activity at 3 mM with feruloyl-CoA as substrate
Phenylglyoxal
47% residual activity at 1 mM with feruloyl-CoA as substrate
phenylmethylsulfonyl fluoride
60% residual activity at 1 mM with feruloyl-CoA as substrate
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
-
-
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
-
-
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
-
-
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
-
-
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
-
-
Woodward's reagent K
54% residual activity at 0.02 mM with feruloyl-CoA as substrate
5-hydroxyferuloyl-CoA
substrate inhibition at high concentration above 60 microM; substrate inhibition at high concentration above 60 microM
feruloyl-CoA
substrate inhibition at high concentration above 60 microM; substrate inhibition at high concentration above 60 microM
additional information
not inhibited by N-ethylmaleimide, 4-hydroxymercurybenzoate, and N-bromosuccinimide
-
additional information
-
not inhibited by N-ethylmaleimide, 4-hydroxymercurybenzoate, and N-bromosuccinimide
-
additional information
-
inhibition by antisense strategy alters lignin content and structure
-
additional information
-
inhibition by antisense strategy alters lignin content and structure
-
additional information
the transcript abundance of CCR can be reduced by 35% in transgenic Norway spruce plants expressing antisense CCR. Down-regulation of CCR results in up to 8% lower lignin content and the apparent contribution of H-lignin to the total lignin decreases. The kappa number of small-scale Kraft pulps is reduced in one CCR down-regulated line
-
additional information
-
the transcript abundance of CCR can be reduced by 35% in transgenic Norway spruce plants expressing antisense CCR. Down-regulation of CCR results in up to 8% lower lignin content and the apparent contribution of H-lignin to the total lignin decreases. The kappa number of small-scale Kraft pulps is reduced in one CCR down-regulated line
-
additional information
CCR is more downregulated in colored than in the white zones of stems of transformants
-
additional information
CCR enzyme activity declines dramatically at the heading and milky stages in stems of the C6001 cultivar
-
additional information
-
CCR enzyme activity declines dramatically at the heading and milky stages in stems of the C6001 cultivar
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
OsRac1
-
interaction with OsRac1, one of the Rac/Rop family of small GTPases, lead to the enzymatic activation of OsCCR1 in vitro
-
additional information
CCR enzyme activity is increased progressively along with lignin biosynthesis and stem maturity. During stem development, CCR1 mRNA levels remain high at elongation, heading, and milky stages in the wheat H4564 cultivar. High CCR1 mRNA levels and high CCR enzyme activity in wheat stem are correlated with a higher Klason lignin content and greater stem mechanical strength in the H4564 cultivar. Escherichia coli BL21(DE3) and BL21(DE3)pLysS strains produce a much higher amount of CCR1 protein compared with the RIL and RP strains
-
additional information
-
CCR enzyme activity is increased progressively along with lignin biosynthesis and stem maturity. During stem development, CCR1 mRNA levels remain high at elongation, heading, and milky stages in the wheat H4564 cultivar. High CCR1 mRNA levels and high CCR enzyme activity in wheat stem are correlated with a higher Klason lignin content and greater stem mechanical strength in the H4564 cultivar. Escherichia coli BL21(DE3) and BL21(DE3)pLysS strains produce a much higher amount of CCR1 protein compared with the RIL and RP strains
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Proteomics unravels new candidate genes for Meloidogyne resistance in wild Arachis.
Infections
Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01595
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.01973
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.0248
4-coumaroyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0316
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.05581
4-coumaroyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.0572
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.11608
4-coumaroyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.1165
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.1265
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.2157
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.2743
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.01885
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.02376
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.0296
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.0376
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.04295
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.09838
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.15233
caffeoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.1817
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.28301
caffeoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.3925
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.00986
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.01431
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.01643
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132T
0.01731
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132S
0.0238
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.0254
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.02759
feruloyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.03123
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155H
0.032
feruloyl-CoA
mutant enzyme S99G, pH and temperature not specified in the publication
0.0356
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.036
feruloyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.039
feruloyl-CoA
mutant enzyme L64W, pH and temperature not specified in the publication
0.042
feruloyl-CoA
mutant enzyme H215L, pH and temperature not specified in the publication
0.047
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.047
feruloyl-CoA
mutant enzyme R51G, pH and temperature not specified in the publication
0.04887
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.057
feruloyl-CoA
mutant enzyme D77G, pH and temperature not specified in the publication
0.06
feruloyl-CoA
mutant enzyme V200E, pH and temperature not specified in the publication
0.07042
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.07474
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant L192M
0.079
feruloyl-CoA
mutant enzyme S212G, pH and temperature not specified in the publication
0.0933
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.096
feruloyl-CoA
mutant enzyme F30V, pH and temperature not specified in the publication
0.102
feruloyl-CoA
mutant enzyme I31N, pH and temperature not specified in the publication
0.13699
feruloyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.166
feruloyl-CoA
mutant enzyme R51G/D77G, pH and temperature not specified in the publication
0.244
feruloyl-CoA
mutant enzyme RF30V/I31N, pH and temperature not specified in the publication
0.01924
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.03494
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.04102
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.05092
sinapoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.0548
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.0565
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.0766
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.1533
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.56836
sinapoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics analysis
-
additional information
additional information
thermodynamics and Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000265
4-coumaroyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0142
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.0183
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.031
4-coumaroyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.188
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.232
4-coumaroyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.32
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.324
4-coumaroyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.0000293
caffeoyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0327
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.0362
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.093
caffeoyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.162
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.23
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.326
caffeoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.559
caffeoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.0101
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132T
0.0192
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132S
0.063
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.136
feruloyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.1409
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155H
0.18
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.24
feruloyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.289
feruloyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.8375
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
1.033
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
1.905
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant L192M
2.01
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
2.1
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
24
feruloyl-CoA
mutant enzyme S212G, pH and temperature not specified in the publication
44
feruloyl-CoA
mutant enzyme H215L, pH and temperature not specified in the publication
84
feruloyl-CoA
mutant enzyme R51G/D77G, pH and temperature not specified in the publication
100
feruloyl-CoA
mutant enzyme R51G, pH and temperature not specified in the publication
108
feruloyl-CoA
mutant enzyme D77G, pH and temperature not specified in the publication
122
feruloyl-CoA
mutant enzyme V200E, pH and temperature not specified in the publication
137
feruloyl-CoA
mutant enzyme F30V, pH and temperature not specified in the publication
142
feruloyl-CoA
mutant enzyme RF30V/I31N, pH and temperature not specified in the publication
144
feruloyl-CoA
mutant enzyme S99G, pH and temperature not specified in the publication
155
feruloyl-CoA
mutant enzyme I31N, pH and temperature not specified in the publication
160
feruloyl-CoA
mutant enzyme L64W, pH and temperature not specified in the publication
162
feruloyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.013
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.052
sinapoyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.064
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.098
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.135
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.2
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.261
sinapoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.829
sinapoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00107
4-coumaroyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
1.28
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
2
4-coumaroyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
4.3
4-coumaroyl-CoA
isoform CCR1, pH and temperature not specified in the publication
1.15
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
2
caffeoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
2.2
caffeoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
1.8
feruloyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
10.5
feruloyl-CoA
isoform CCR1, pH and temperature not specified in the publication
18.26
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
72.19
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
310
feruloyl-CoA
mutant enzyme S212G, pH and temperature not specified in the publication
510
feruloyl-CoA
mutant enzyme R51G/D77G, pH and temperature not specified in the publication
590
feruloyl-CoA
mutant enzyme RF30V/I31N, pH and temperature not specified in the publication
1000
feruloyl-CoA
mutant enzyme H215L, pH and temperature not specified in the publication
1400
feruloyl-CoA
mutant enzyme F30V, pH and temperature not specified in the publication
1500
feruloyl-CoA
mutant enzyme I31N, pH and temperature not specified in the publication
1900
feruloyl-CoA
mutant enzyme D77G, pH and temperature not specified in the publication
2000
feruloyl-CoA
mutant enzyme V200E, pH and temperature not specified in the publication
2100
feruloyl-CoA
mutant enzyme R51G, pH and temperature not specified in the publication
4100
feruloyl-CoA
mutant enzyme L64W, pH and temperature not specified in the publication
4500
feruloyl-CoA
mutant enzyme S99G, pH and temperature not specified in the publication
4600
feruloyl-CoA
wild type enzyme, pH and temperature not specified in the publication
1.5
sinapoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
1.56
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
5.2
sinapoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0157
5-hydroxyferuloyl-CoA
competitive inhibition of 5-hydroxyferuloyl-CoA on the feruloyl-CoA reaction
0.0153
caffeoyl-CoA
competitive inhibition of caffeoyl-CoA on the feruloyl-CoA reaction
0.031 - 0.156
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
0.0071 - 0.055
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
0.0044 - 0.057
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
0.212 - 0.422
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
0.068 - 0.29
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
0.02
sinapoyl-CoA
competitive inhibition of sinapoyl-CoA on the feruloyl-CoA reaction
0.0063
feruloyl-CoA
competitive inhibition of feruloyl-CoA on the 5-hydroxyferuloyl-CoA reaction
0.0066
feruloyl-CoA
competitive inhibition of feruloyl-CoA on the sinapoyl-CoA reaction
0.0083
feruloyl-CoA
competitive inhibition of feruloyl-CoA on the caffeoyl-CoA reaction
0.031
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
-
with feruloyl-CoA as substrate, uncompetitive inhibition
0.156
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
-
with sinapoyl-CoA as substrate, uncompetitive inhibition
0.0071
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
-
with sinapoyl-CoA as substrate, noncompetitive inhibition
0.055
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
-
with feruloyl-CoA as substrate, uncompetitive inhibition
0.0044
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
-
with feruloyl-CoA as substrate, noncompetitive inhibition
0.057
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
-
with sinapoyl-CoA as substrate, noncompetitive inhibition
0.212
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
-
with sinapoyl-CoA as substrate, uncompetitive inhibition
0.422
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
-
with feruloyl-CoA as substrate, uncompetitive inhibition
0.068
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
-
with sinapoyl-CoA as substrate, noncompetitive inhibition
0.29
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
-
with feruloyl-CoA as substrate, uncompetitive inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.25
6.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
when the pH is above 6.5, the activity becomes negligible, feruloyl-CoA as substrate
5.4 - 8
-
pH 5.4: about 10% of activity maximum, pH 8.0: about 15% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
25
-
below and above 25°C, gradual loss in the enzyme activity is recorded
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
10 - 60
activity range, profile overview, the enzyme is active even below 10°C
10 - 60
the enzyme activity is optimal at 30°C, with a steep decrease when the reaction is performed at 40°C. Isoform CCR1 exhibits relatively high activity at low temperature
10 - 60
the enzyme shows approximately 50% activity at 60°C, approximately 5.3% activity at 20°C and no activity at 10°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Fragaria chiloensis x Fragaria virginiana, cv. Elsanta
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
strong enzyme expression in turning and red ripe fruits. The CCR gene shows higher expression levels in varieties that produce fruits with soft tissue
brenda
differential expression level of CCR between freshly harvested and stored fruits as well as between fruits stored under various storage conditions. A high VcCCR transcript level is detected in freshly harvested blueberry fruits and fruits stored at 24% CO2 + 18% O2, while VcCCR is expressed at low levels in blueberry fruits stored at 6% CO2 + 18% O2, 18% CO2 +18% O2 and cold storage
brenda
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inoculated with Agrobacterium rhizogenes, maximum activity 8 days after inoculation
brenda
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strong and transient increase of AtCCR2 mRNA after inoculation with Xanthomonas campestris pv. campestris, northern blot analysis
brenda
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CCR1 is expressed basipetally in the leaf, CCR1 expression is developmentally regulated in leaves,overview. Leaves on day 9 show CCR1 expression strongly at the tip, mildly in the middle, and no expression at the proximal regions
brenda
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CCR1 is expressed basipetally in the leaf, CCR1 expression is developmentally regulated in leaves,overview. Leaves on day 9 show CCR1 expression strongly at the tip, mildly in the middle, and no expression at the proximal regions
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brenda
gene expression analysis reveals that HcCCR1 is highly upregulated in mature leaves of 16-week-old plants
brenda
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gene expression analysis reveals that HcCCR1 is highly upregulated in mature leaves of 16-week-old plants
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brenda
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the CCR2 gene, which is not expressed in wild-type stems, is found to be expressed in the stems of two CCR1 mutants
brenda
HcCCR1 shows a lower expression in 2-week-old stems, is sharply upregulated at 4 weeks, and is then gradually downregulated. Transcript expression patterns of HcCCR1 in various tissues and organs during developmental stages, overview
brenda
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HcCCR1 shows a lower expression in 2-week-old stems, is sharply upregulated at 4 weeks, and is then gradually downregulated. Transcript expression patterns of HcCCR1 in various tissues and organs during developmental stages, overview
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brenda
additional information
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CCR1 is a developmentally regulated gene, whose basipetally ordered expression pattern perfectly matches that of exit from the cell proliferation phase during leaf development
brenda
additional information
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CCR1 is a developmentally regulated gene, whose basipetally ordered expression pattern perfectly matches that of exit from the cell proliferation phase during leaf development
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brenda
additional information
relative expression profiles of monolignol biosynthesis genes in vegetative tissues, flowers, and fruit developmental stages of Fragaria ananassa cv.Elsanta
brenda
additional information
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relative expression profiles of monolignol biosynthesis genes in vegetative tissues, flowers, and fruit developmental stages of Fragaria ananassa cv.Elsanta
brenda
additional information
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developing root tissue shows a higher level of CCR content and lignin deposition than stem, expression pattern of CCR protein in developing control seedlings, overview
brenda
additional information
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the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
brenda
additional information
the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
brenda
additional information
the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
HcCCR1 does not contain any transmembrane helices and is therefore assumed to be localized in cytosol
brenda
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HcCCR1 does not contain any transmembrane helices and is therefore assumed to be localized in cytosol
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
evolution
the conserved motifs G-X-X-G-X-X-A and D-X-X-D are reported to be involved in NAD(P) binding and adenine binding pocket stabilization. In addition, the NADP specificity motif R(X)5K is identified, which is a key structure that distinguishes CCR from other NAD(H)-dependent SDRs. Sequence comparisons and phylogenetic analysis of Populus tometosa CCRs, overview. Of the 11 PtoCCR and PtoCCR-like proteins, PtoCCR1 and 7 each catalyze at least one substrate. PtoCCR1 is active only with feruloyl-CoA as a substrate, while PtoCCR7 accepts all hydroxycinnamoyl-CoA esters
evolution
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phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
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malfunction
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Ccr1 knockout mutants exhibit a dramatic decrease in S lignin in vascular tissue
malfunction
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in the ccr1 mutant, CCR1 gene expression is reduced to 31% of the residual wild type level leading to a decrease in lignin content and significant changes in lignin structure. 4-hydroxyphenyl units are strongly decreased and the syringyl/guaiacyl ratio is slightly increased. Down-regulation of CCR1 alters schlerenchymatic fibre morphology and cell wall structure. Moderate down-regulation of CCR1 significantly improves cell wall digestibility in maize
malfunction
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20 month-old trees transgenic trees with downregulated CCR enzymes show up to 161% increased ethanol yield from tissues including bark, generated from the lignocellulosic biomass, strong downregulation of CCR also affects biomass yield. Wood samples derived from the transgenic trees are more easily processed into ethanol than wild-type. The improved saccharification yield is due to a higher cellulose conversion and correlates with the abundance of ferulic acid markers
malfunction
AtCCR2 expression is increased in Arabidopsis ccr1 mutant and function is partly compensated
malfunction
Betula platyphylla x Betula pendula
BpCCR1 overexpression increases lignin content up to 14.6%, and its suppression decreases lignin content by 6.3%. Modification of BpCCR1 expression leads to conspicuous changes in wood characteristics, including xylem vessel number and arrangement, and secondary wall thickness. The growth of transgenic trees in terms of height is also significantly influenced by the modification of BpCCR1 genes. The secondary xylem microstructures of stems base is altered with thicker cell walls of xylem fibers, penotype, overview
malfunction
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ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
malfunction
levels of G-monomers are considerably reduced in FaCCR-silenced fruits. Phenotypic analysis shows that the texture of the fruits injected with different FaCCR constructs is more solid than that of the untreated fruits , but up- or downregulation of the enzyme does not alter the red color and appearance of the fruits
malfunction
T154Y mutation in SbCCR1 leads to broader substrate specificity and faster turnover
malfunction
the positively charged extended structure of His208 was important in stabilizing CoA, while the mutants (M208, V208, and Y208) were unable to assume this function
malfunction
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enzyme downregulation increases the biosynthesis of phenolic acids
malfunction
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enzyme knockdown transgenics display a decrease in root and anther lignin depositions. Isoform CCR14 knockdown transgenics display loss of lignification in their anthers
malfunction
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suppression of enzyme gene expression results in a reduction in cinnamyl alcohol dehydrogenase enzyme activity in stem-differentiating xylem
malfunction
truncated enzyme lines (CCR-3, CCR-7 and CCR-12) show marked reduction in guaiacyl lignin which is reduced by 10.2% in both CCR-3 and CCR-7, and 9.3% in CCR-12. The down-regulation of lignin leads to significant increase in total phenolics content than the wild type control
malfunction
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ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
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metabolism
the enzyme carries out the first committed step in monolignol biosynthesis and acts as a first regulatory point in lignin formation
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
cinnamoyl-CoA reductase (CCR) is the first enzyme in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis. It is likely that Mt-CCR1 is the major CCR isozyme involved in lignin biosynthesis, and Mt-CCR2 is proposed to be involved in an alternative route for S lignin biosynthesis in Medicago truncatula
metabolism
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enzyme cinnamoyl-CoA reductase (CCR) catalyzes the first step in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
Betula platyphylla x Betula pendula
the enzyme is a key enzyme involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in the Monolignol biosynthetic pathway in dicotyledonous angiosperms, pathway overview
metabolism
the enzyme is involved in the the monolignol biosynthetic pathway
metabolism
the formation of 4-hydroxycinnamaldehydes is catalyzed by 4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR). 4-Hydroxycinnamaldehydes are a class of natural plant secondary products that includes coniferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffealdehyde. They are involved in several secondary metabolism pathways, such as those involved in the biosynthesis of phenolic acids, monolignols, flavonoids and terpenoids. 4-Hydroxycinnamaldehydes are also key intermediates in the biosynthesis and degradation of lignins, which protect cell wall polysaccharides from microbial degradation
metabolism
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
metabolism
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cinnamoyl CoA reductase is the dedicated enzyme in the lignin pathway
metabolism
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isoform CCR14 is a substrate of the SCF(FBK1) E3 ligase complex, and its degradation is mediated by the 26S proteasome
physiological function
CCR is responsible for the CoA ester conversion into aldehyde in monolignol biosynthesis, which diverts phenylpropanoid-derived metabolites into the biosynthesis of lignin. Lignifications in blueberry fruits are regulated under various post-harvest conditions
physiological function
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cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
physiological function
cinnamoyl-CoA reductase catalyzes the reduction of cinnamoyl-CoA esters to their respective cinnamaldehydes and is considered as a key enzyme in lignin formation
physiological function
cinnamoyl-coenzyme A reductase (CCR) catalyzes the reduction of hydroxycinnamoyl-CoA esters using NADPH to produce hydroxycinnamyl aldehyde precursors in lignin synthesis. Isozyme SbCCR2 displays greater activity toward 4-coumaroyl-CoA than does isozyme SbCCR1, which implies a role in the synthesis of defense-related lignin. CCR1 is involved in lignification of stem tissues, whereas CCR2 is involved in lignification in response to attack by pathogens
physiological function
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enzyme CCR is involved in lignin biosynthesis and might be playing a role in drought and salinity stress
physiological function
Betula platyphylla x Betula pendula
specific functions of a birch enzyme CCR1 in wood formation and growth
physiological function
the enzyme is involved in drought defense
physiological function
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isoform CCR20 is primarily involved in developmental deposition of lignins in secondary cell walls
physiological function
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vessel-specific reintroduction of isoform CCR1 in dwarfed ccr1 mutants restores vessel and xylary fiber integrity and increases biomass
physiological function
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cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
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additional information
active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
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active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
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structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
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structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
additional information
the substrate-binding domain of the SbCCR1 is surrounded by two groups of a-helices, and the floor of the substrate-binding pocket is largely composed of beta-strands. Residues T154 and Y310 ae involved in substrate binding with ferulic acid, Tyr310 binds the 4-hydroxyl of feruloyl-CoA, while Thr154 binds the 3-methoxy group of this molecule. Molecular docking and modelling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
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Show AA Sequence and Transmembrane Helices (157 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
37500
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
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x * 37900, isoform CCR17, calculated from amino acid sequence
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x * 37900, isoform CCR21, calculated from amino acid sequence
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x * 38600, isoform CCR19, calculated from amino acid sequence
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x * 38700, isoform CCR20, calculated from amino acid sequence
additional information
the enzyme contains two highly conserved motifs:NAD(P) binding domain (VTGAGGFIASWMVKLLLEKGY) at N-terminal and probable catalytic domain (NWYCYGK)
additional information
the enzyme contains two highly conserved motifs:NAD(P) binding domain (VTGAGGFIASWMVKLLLEKGY) at N-terminal and probable catalytic domain (NWYCYGK)
additional information
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the enzyme contains two highly conserved motifs:NAD(P) binding domain (VTGAGGFIASWMVKLLLEKGY) at N-terminal and probable catalytic domain (NWYCYGK)
additional information
the native protein possesses four Trp residues exposed on the surface and 66% of helical structure, analysis of different enzyme structures by UV-circular dichroism and Rayleigh light scattering, detailed overview
additional information
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the native protein possesses four Trp residues exposed on the surface and 66% of helical structure, analysis of different enzyme structures by UV-circular dichroism and Rayleigh light scattering, detailed overview
additional information
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the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
three-dimensional enzyme structure analysis and comparisons, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
lipoprotein
the HcCCR1 protein contains a palmitoylation site in the HcCCR1 protein
lipoprotein
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the HcCCR1 protein contains a palmitoylation site in the HcCCR1 protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with NADP+, hanging drop, vapor diffusion method, mixing of 20 mg/ml protein in 20 mM Tris base, pH 7.5, 2 mM DTT, and 1 mM NADP+, with an equal volume of reservoir solution , containing 100 mM Bis-Tris, pH 6.5, and 25% w/v PEG 3350, and equilibration against reservoir solution at 4°C, X-ray diffraction structure determination and analysis at 2.35 A resolution, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D77G
D77N
the mutant has same substrate affinity (feruloyl CoA) as that of wild type enzyme
F30V
F30V/I31N
the mutant shows approximately 7fold increase in Km and 8fold decrease in kcat/Km values
H215L
I131N
the mutant shows slightly reduced catalytic efficiency compared to the wild type
I31F
the mutant shows more negative binding energy for hydroxyferuloyl CoA
I31M
the mutant exhibits equal affinity for coumaroyl and hydroxyferulol CoA
I31N
K174M
K174N
the mutant has favorable binding energy for hydroxyferuloyl-CoA
K174R
the mutant has favorable binding energy for hydroxyferuloyl-CoA
L64W
the mutant shows no significant change in Km values compared to the wild type enzyme
R51G
R51G/D77G
the mutant displays 5fold increase in Km and around 9fold reduction in specificity constant
S136A
S212G
S99G
the mutant shows no significant change in Km values compared to the wild type enzyme
V200A
the mutant displays substrate specificity towards coumaroyl-CoA
V200E
V200G
the mutant displays substrate specificity towards coumaroyl-CoA
Y170C
the mutant displays less number of interactions compared to the wild type enzyme
Y170H
A132S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A132T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A43V
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F155H
site-directed mutagenesis, the mutant is only active with feruloyl-CoA as substrate in contrast to the wild-type enzyme
F155Y
site-directed mutagenesis, the mutant exhibits greater catalytic efficiency for sinapoyl-CoA compared to the wild-type PtoCCR7
L192M
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
S123T
the mutant shows reduced activity compared to the wild type enzyme
T154A
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
T154Y
the mutation in SbCCR1 leads to broader substrate specificity and faster turnover. The T154Y mutant exhibits 4.9 and 144fold increases in catalytic efficiency for feruloyl-CoA and 4-coumaroyl-CoA, respectively, over those of wild-type SbCCR1
Y310F
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
additional information
D77G
site-directed mutagenesis, structure comparison to the wild-type enzyme
D77G
the mutant displays equal affinity for caffeoyl-CoA and sinapoyl-CoA
D77G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
F30V
site-directed mutagenesis, structure comparison to the wild-type enzyme
F30V
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
H215L
site-directed mutagenesis, structure comparison to the wild-type enzyme
H215L
the mutant shows no significant change in Km values compared to the wild type enzyme
I31N
site-directed mutagenesis, structure comparison to the wild-type enzyme
I31N
the mutant demonstrates better affinity for sinapoyl CoA over others
K174M
site-directed mutagenesis, structure comparison to the wild-type enzyme
K174M
the mutant shows complete loss of activity with feruloyl-CoA as substrate
R51G
site-directed mutagenesis, structure comparison to the wild-type enzyme
R51G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
R51G
the mutation alters side chain from polar charged to small compact neutral residue, resulting in marked decrease in accessible surface area and leads to loss of interactions with substrate
S136A
site-directed mutagenesis, structure comparison to the wild-type enzyme
S136A
the mutant shows complete loss of activity with feruloyl-CoA as substrate
S212G
site-directed mutagenesis, structure comparison to the wild-type enzyme
S212G
the mutant exhibits the catalytic efficiencies less than 10% of wild type enzyme
S212G
the mutant shows a 2.5fold increase in Km, 7fold reduction in kcat and 15fold decrease in kcat/Km
V200E
site-directed mutagenesis, structure comparison to the wild-type enzyme
V200E
the mutant shows reduced catalytic efficiency compared to the wild type
Y170H
site-directed mutagenesis, structure comparison to the wild-type enzyme
Y170H
the mutant shows complete loss of activity with feruloyl-CoA as substrate
additional information
in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
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two knockout mutants for CCR1. Both have a dwarf phenotype and a delayed senescence. At complete maturity, their inflorescence stems display a 25-35% decreased lignin level, some alterations in lignin structure with a higher frequency of resistant interunit bonds and a higher content in cell wall-bound ferulic esters. Ferulic acid-coniferyl alcohol ether dimers in cell walls show similar levels in wild-type and mutant plants. Expression of CCR2, involved in plant defense, is increased in the mutants and can account for the biosynthesis of lignins in the CCR1-knockout plants. CCR1-mutant plantlets have 3 to 4times less sinapoyl malate than controls and accumulate some feruloyl malate. The same compositional changes occurr in the rosette leaves of greenhouse-grown plants. Relative to the control, stems accumulate unusually high levels of both sinapoyl malate and feruloyl malate as well as more kaempferol glycoside
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
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additional information
Betula platyphylla x Betula pendula
construction of enzyme overexpression and suppression lines, vector transfection using Agrobacterium tumefaciens strain EHA105
additional information
gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR) are fused by means of genetic engineering to generate an artificial bifunctional enzyme. Chimeric 4CL1-CCR is overexpressed in Escherichia coli supplemented with phenylpropanoic acids. Three 4-hydroxycinnamaldehydes, p-coumaraldehyde, caffealdehyde and coniferaldehyde, are thereby biosynthesized and secreted into the culture medium. Extracellular hydroxycinnamoyl-CoA thioesters are not detected, hydroxycinnamoyl-CoA thioesters accumulate only in the cell, because they cannot freely pass through the cellular membrane. The fusion enzyme 4CL1-CCR can catalyze sequential multistep reactions, thereby avoiding the permeability problem of intermediates, which reveals its superiority over a mixture of individual native enzymes. The bifunctional enzyme 4CL1-CCR plays a central role in cellular metabolism by converting phenylpropanoic acids to their corresponding cinnamaldehydes
additional information
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construction of genetically modified poplars, that are downregulated for cinnamoyl-CoA reductase (CCR). 20 month-old trees transgenic trees with downregulated CCR enzymes show up to 161% increased ethanol yield from tissues including bark, generated from the lignocellulosic biomass, strong downregulation of CCR also affects biomass yield. Wood samples derived from the transgenic trees are more easily processed into ethanol than wild-type
additional information
in CCR-deficient poplar, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 8
Ll-CCRH1 is transformed into acid induced (pH 2.0) molten globule like structure, exhibiting altered secondary structure, diminished tertiary structure and exposed hydrophobic residues. The molten globule like structure is examined for the thermal and chemical stability. The altered secondary structure of L1-CCRH1 at pH 2.0 is stable up to 90°C. In presence of 0.25 M guanidine hydrochloride (GdnHCl), it gets transformed into different structure which is stable in the vicinity of 2 M GdnHCl (as compared to drastic loss of native structure in 2 M GdnHCl) as seen in far UV-CD spectra. The structural transition of Ll-CCRH1 at pH 2.0 followed another transition after readjusting the pH to 8.0, forming a structure with hardly any similarity to that of native protein
742677
6 - 7
-
the enzyme is most stable around pH 6.5 at 25°C for 90 min, while at pH 6.0 and 7.0, the enzyme is stable for 45 and 60 min, respectively
725147
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
the enzyme is stable for 60 min at 25°C and at optimum temperature 30°C, stability is observed for 40 min. However, at 20°C and 35°C, 36% and 42% loss in activity is observed after 60 min. Above 40°C, significant loss in Ll-CCRH1 activity is observed within 30 min
20 - 90
the native enzyme undergoes rapid structural transitions at and above 45°C and starts forming aggregates at 55°C, the acid induced molten globule state state of the enzyme structure is stable up to 90°C, overview
additional information
additional information
-
CCR1 melting temperature is 35°C in absence of ligands and 42-47 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Medicago truncatula CCR2 isozyme, overview
additional information
CCR1 melting temperature is 35°C in absence of ligands and 42-47 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Medicago truncatula CCR2 isozyme, overview
additional information
CCR1 melting temperature is 33°C in absence of ligands and 43-45 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Petunia hybrida CCR1 isozyme, overview
additional information
-
CCR1 melting temperature is 33°C in absence of ligands and 43-45 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Petunia hybrida CCR1 isozyme, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol: stabilizes , only stable in presence of
ethyleneglycol, 15%, stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CCR protein is purified using a Bug-Buster GSTclosed circleBind purification kit, and the fused tag is cleaved and removed using the Enterokinase Cleavage capture kit
Ni-NTA agarose column chromatography
recombinant fusion proteins GST-AtCCR1 and GST-AtCCR2, expressed in Escherichia coli
-
recombinant His-tagged enzyme CCR from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme CCR1 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His-tagged enzyme CCR1 from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, anion exchange chromatography, and dialysis
recombinant His-tagged wild-type and mutant enzymes CCR7 from Escherichia coli strain M15 by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
using a glutathione-sepharose 4 Fast Flow column, purified GST-AtCCR1 is cleaved by thrombin to remove the GST tag
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CCR, recombinant expression of His-tagged enzyme CCR in Escherichia coli, coexpression with 4-coumarate-CoA ligase, EC 6.2.1.12. The best expression conditions for recombinant PtCCR are 6 h of 0.4 mM IPTG induction at 37°C
cloned into the pET-29b vector and expressed in Escherichia coli strains BL21(DE3), BL21(DE3)pLysS, RIL, and RP
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli M15 cells
expressed in Nicotiana tabacum variety Xanthi via Agrobacterium tumefaciens strain LBA4404
-
five-year-old transgenic plants of Norway spruce Picea abies expressing the Norway spruce gene encoding CCR in antisense orientation under the control of the maize ubiquitin promoter
for generation of RNAi constructs and for tomato transformation through Agrobacterium tumefaciens, into the pGEX4T-1 vector for expression in Escherichia coli BL21 cells
for the construction of a yeast two-hybrid assay prey vectors containing different fragments of OsCCR1 are made by using the pVP16 vector, for transient expression in rice protoplasts a OsCCR1-GFP construct is generated, full length OsCCR1 is cloned into a pET30 vector for expression in Escherichia coli cells
-
gene CCR, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis by differential display reverse transcription-polymerase chain reaction, DDRT-PCR, recombinant expression in Escherichia coli
gene CCR, recombinant overexpression of chimeric 4CL1-CCR in Escherichia coli strain M15 supplemented with phenylpropanoic acids. Three 4-hydroxycinnamaldehydes, p-coumaraldehyde, caffealdehyde and coniferaldehyde, are thereby biosynthesized and secreted into the culture medium, identification of phenylpropanoic acids and 4-hydroxycinnamaldehydes by HPLCPDAESIMSn
gene CCR, sequence comparisons and phylogenetic analysis
gene CCR1, DNA and amino acid sequence determination and analysis of diverse isozymes from Populus tomentosa, phylogenetic analysis, recombinant expression of His-tagged isozyme CCR1 in Escherichia coli strain M15, subcloning in Escherichia coli strain DH5alpha
gene CCR1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
Betula platyphylla x Betula pendula
gene CCR1, recombinant expression of His6-tagged enzyme in Escherichia coli
gene CCR1, recombinant His-tagged enzyme expression in Escherichia coli strain Rosetta (DE3)
gene CCR1, the gene locus maps to chromosome 1, DNA and amino acid sequence determination and analysis
-
gene CCR7, DNA and amino acid sequence determination and analysis of diverse isozymes from Populus tomentosa, phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant isozymes CCR7 in Escherichia coli strain M15, subcloning in Escherichia coli strain DH5alpha
gene FaCCR, DNA and amino acid sequence determination and analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene HcCCR1, sequence comparisons and phylogenetic analysis, quantitative gene expression analysis
gene SbCCR1, DNA and amino acid sequence determination and analysis, cloning and expression in Escherichia coli strain DH5alpha, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Nicotiana benthaminana leaves via Agrobacterum tumefaciens transfection, quantitative real-time PCR enzyme expression analysis
gene SbCCR2-1, DNA and amino acid sequence determination and analysis, cloning and expression in Escherichia coli strain DH5alpha, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Nicotiana benthaminana leaves via Agrobacterum tumefaciens transfection, quantitative real-time PCR enzyme expression analysis
gene SbCCR2-2, DNA and amino acid sequence determination and analysis, cloning and expression in Escherichia coli strain DH5alpha, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Nicotiana benthaminana leaves via Agrobacterum tumefaciens transfection, quantitative real-time PCR enzyme expression analysis
heterologous expression as His-tagged fusion protein in Escherichia coli
into the pET41a+ and pET23b+ vector for expression in Escherichia coli BL21DE3 cells
into the pGEX-4T vector for expression in Escherichia coli BL21DE3 cells
-
introduction of four different constructs into poplar (Populus tremula x Populus alba)
isoforms CCR17, CCR19, CCR20, and CCR21 are expressed in Escherichia coli BL21(DE3) cells
-
specific PCR product is cloned into the pGEM-T Easy vector, as an expression vector for Escherichia coli, pET28a is used
two genes AtCCR1 and AtCCR2, localised on chromosome 1, AtCCR1 is associated with lignin biosynthesis during development, AtCCR2 is associated with the hypersensitive response to pathogen attack
-
two genes ZmCCR1 and ZmCCR2, ZmCCR1 is involved in constitutive lignification, function of ZmCCR2 unknown
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CCR protein is reduced in NaCl treated stems and corresponding lignin deposition is also low
-
developmental- and stress-mediated expression of cinnamoyl-CoA reductase in Hibiscus cannabinus. HcCCR2 is expressed differentially in response to various stresses, and the highest expression is observed by drought and NaCl treatments
developmental- and stress-mediated expression of cinnamoyl-CoA reductase in Hibiscus cannabinus. HcCCR2 is expressed differentially in response to various stresses, and the highest expression is observed by drought and NaCl treatments, transcript expression patterns of HcCCR2 in response to various abiotic stresses, overview
enzyme expression can be induced by exposure to Xanthomonas campestris pv. Campestris or methyl jasmonate. Enzyme expression is highest in old roots, flowers, and young leaves
gene expression analysis reveals that HcCCR1 is highly upregulated in mature leaves of 16-week-old plants. The enzyme expression is also transiently upregulated by cold and drought, as well as salt (NaCl) treatment. The enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated. The enzyme is permantly upregulated by H2O2 for more than 48 h
knockout of caffeoyl CoA 3-O-methyltransferase up-regulates isoform CCR2
-
no significant induction of FaCCR gene in the fruits exposed to Agrobacterium, ascompared to control fruits during 4 days. The expression level can even be reduced upon agroinfiltration
significantly down-regulated in the rain shelter group compared to those in the control group
soluble ferulic acid in leaf cells is closely negatively correlated with CCR1 expression
the enzyme expression is induced upon stress by salt, drought, abscisic acid, and wounding, as well as by cold, H2O2, methyljasmonate, and salicylic acid
the enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated
the enzyme is induced by drought treatment, genes SbCCR1 and SbCCR2-2 mainly respond in the first phase of drought defense, while the SbCCR2-1 gene responds during the whole drought defense period
the enzyme is induced by mannitol in stems leading to increased enzyme protein content and lignin deposition
-
the expressions of isoforms CCR17 and 21 are induced in response to biotic and abiotic stresses, such as Magnaporthe grisea and Xanthomonas oryzae pv. oryzae infections, UV-irradiation and high salinity (250 mM NaCl)
-
the HcCCR1 gene is modulated by different external stresses, overview
gene expression analysis reveals that HcCCR1 is highly upregulated in mature leaves of 16-week-old plants. The enzyme expression is also transiently upregulated by cold and drought, as well as salt (NaCl) treatment. The enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated. The enzyme is permantly upregulated by H2O2 for more than 48 h
gene expression analysis reveals that HcCCR1 is highly upregulated in mature leaves of 16-week-old plants. The enzyme expression is also transiently upregulated by cold and drought, as well as salt (NaCl) treatment. The enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated. The enzyme is permantly upregulated by H2O2 for more than 48 h
-
-
soluble ferulic acid in leaf cells is closely negatively correlated with CCR1 expression
-
soluble ferulic acid in leaf cells is closely negatively correlated with CCR1 expression
-
-
the enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated
the enzyme is first transiently downregulated by methyljasmonate and abscisic acid, after 12 h is becomes transiently upregulated
-
-
the HcCCR1 gene is modulated by different external stresses, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
biotechnology
industry
synthesis
additional information
biotechnology
-
CCR downregulation may become a successful strategy to improve biomass processing if the variability in down-regulation and the yield penalty can be overcome
biotechnology
potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants
biotechnology
potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants
industry
down-regulated CCR lines with a reduced kappa number of small-scale Kraft pulps may be a starting point for constructing double mutants with enhanced properties of significance for practical forestry
industry
downregulation of CCR in transgenic poplar (Populus tremula x Populus alba) is associated with up to 50% reduced lignin content and an orange-brown, often patchy, coloration of the outer xylem. Lignin is relatively more reduced in syringyl than in guaiacyl units. Elevated ferulic acid levels, ferulic acid is incorporated into the lignin via ether bonds. Reduced levels of lignin and hemicellulose are associated with an increased proportion of cellulose. Stress response induced by altered cell wall structure. Chemical pulping of wood derived from 5-year-old, field-grown transgenic lines reveal improved pulping characteristics, but growth is affected in all transgenic lines tested. Trees harboring CCR alleles that result in reduced CCR activity are interesting progenitors for breeding programs. The lower lignin and hemicellulose levels and associated relative increase in cellulose suggest that CCR downregulation may be a good strategy to improve plant biomass for bioethanol production
synthesis
potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants
synthesis
potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants
additional information
CCR1 is present as a single-copy gene in the wheat genome. It groups together with other monocot CCR sequences while it diverges from CCR2. It may be involved in the regulation of lignin biosynthesis during stem maturity and may contribute to stem strength support in wheat
additional information
-
CCR1 is present as a single-copy gene in the wheat genome. It groups together with other monocot CCR sequences while it diverges from CCR2. It may be involved in the regulation of lignin biosynthesis during stem maturity and may contribute to stem strength support in wheat
additional information
-
the thioacidolysis monomer 1,2,2-trithioethyl ethylguaiacol is a general marker for incorporation of ferulic acid into the lignification process, and is an indicator that can be used judiciously for CCR downregulation in a variety of plants as long as the background levels in control materials are measured
additional information
the thioacidolysis monomer 1,2,2-trithioethyl ethylguaiacol is a general marker for incorporation of ferulic acid into the lignification process, and is an indicator that can be used judiciously for CCR downregulation in a variety of plants as long as the background levels in control materials are measured
additional information
the thioacidolysis monomer 1,2,2-trithioethyl ethylguaiacol is a general marker for incorporation of ferulic acid into the lignification process, and is an indicator that can be used judiciously for CCR downregulation in a variety of plants as long as the background levels in control materials are measured
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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1984
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1976
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172
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Enzymic synthesis of lignin precursors. Comparison of cinnamoyl-CoA reductase and cinnamyl alcohol:NADP+ dehydrogenase from spruce (Picea abies L.) and soybean (Glycine max L.)
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1981
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54
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1975
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Purification and characterization of cinnamoyl-CoA reductase from Eucalyptus gunnii
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69
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Eucalyptus gunnii
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Goffner, D.; Grima-Pettenati, J.; Feuillet, C.; Boudet, A.M.
Cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase: Characterization at the biochemical and molecular level of two enzymes involved in lignin synthesis
Colloq. Inst. Natl. Rech. Agron.
69
331-332
1995
Eucalyptus gunnii
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NMR characterization of altered lignins extracted from tobacco plants down-regulated for lignification enzymes cinnamyl-alcohol dehydrogenase and cinnamoyl-CoA reductase
Proc. Natl. Acad. Sci. USA
95
12803-12808
1998
Nicotiana tabacum
brenda
Pincon, G.; Chabannes, M.; Lapierre, C.; Pollet, B.; Ruel, K.; Joseleau, J.P.; Boudet, A.M.; Legrand, M.
Simultaneous down-regulation of caffeic/5-hydroxy ferulic acid-O-methyltransferase I and cinnamoyl-coenzyme A reductase in the progeny from a cross between tobacco lines homozygous for each transgene. Consequences for plant development and lignin synthesis
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126
145-155
2001
Nicotiana tabacum
brenda
Lauvergeat, V.; Lacomme, C.; Lacombe, E.; Lasserre, E.; Roby, D.; Grima-Pettenati, J.
Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria
Phytochemistry
57
1187-1195
2001
Arabidopsis thaliana
brenda
Pichon, M.; Courbou, I.; Beckert, M.; Boudet, A.M.; Grima-Pettenati, J.
Cloning and characterization of two maize cDNAs encoding cinnamoyl-CoA reductase (CCR) and differential expression of the corresponding genes
Plant Mol. Biol.
38
671-676
1998
Zea mays
brenda
Rhodes, Michael J.C.; Wooltorton, Leonard S.C.
Enzymes involved in the reduction of ferulic acid to coniferyl alcohol during the aging of disks of swede root tissue
Phytochemistry
14
1235-1240
1975
Brassica napus subsp. rapifera
-
brenda
Larsen, K.
Molecular cloning and characterization of cDNAs encoding cinnamoyl CoA reductase (CCR) from barley (Hordeum vulgare) and potato (Solanum tuberosum)
J. Plant Physiol.
161
105-112
2004
Solanum tuberosum (Q8H1H6), Solanum tuberosum, Hordeum vulgare (Q8H1H7), Hordeum vulgare
brenda
Ruelland, E.; Campalans, A.; Selman-Housein, G.; Puigdomenech, P.; Rigau, J.
Cellular and subcellular localization of the lignin biosynthetic enzymes caffeic acid-O-methyltransferase, cinnamyl alcohol dehydrogenase and cinnamoyl-coenzyme A reductase in two monocots, sugarcane and maize
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117
93-99
2003
Saccharum officinarum, Zea mays
-
brenda
Larsen, K.
Cloning and characterization of a ryegrass (Lolium perenne) gene encoding cinnamoyl-CoA reductase (CCR)
Plant Sci.
166
569-581
2004
Lolium perenne (Q9FUW8)
brenda
Ma, Q.H.; Tian, B.
Biochemical characterization of a cinnamoyl-CoA reductase from wheat
Biol. Chem.
386
553-560
2005
Triticum aestivum (Q4KUK8), Triticum aestivum
brenda
Thumma, B.R.; Nolan, M.F.; Evans, R.; Moran, G.F.
Polymorphisms in cinnamoyl CoA reductase (CCR) are associated with variation in microfibril angle in Eucalyptus spp
Genetics
171
1257-1265
2005
Eucalyptus sp.
brenda
van der Rest, B.; Danoun, S.; Boudet, A.M.; Rochange, S.F.
Down-regulation of cinnamoyl-CoA reductase in tomato (Solanum lycopersicum L.) induces dramatic changes in soluble phenolic pools
J. Exp. Bot.
57
1399-1411
2006
Solanum lycopersicum (Q4U1I4), Solanum lycopersicum (Q4U1I5), Solanum lycopersicum
brenda
Li, L.; Cheng, X.; Lu, S.; Nakatsubo, T.; Umezawa, T.; Chiang, V.L.
Clarification of cinnamoyl co-enzyme A reductase catalysis in monolignol biosynthesis of Aspen
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46
1073-1082
2005
Populus tremuloides (Q9M631)
brenda
Laskar, D.D.; Jourdes, M.; Patten, A.M.; Helms, G.L.; Davin, L.B.; Lewis, N.G.
The Arabidopsis cinnamoyl CoA reductase irx4 mutant has a delayed but coherent (normal) program of lignification
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48
674-686
2006
Arabidopsis thaliana
brenda
Baltas, M.; Lapeyre, C.; Bedos-Belval, F.; Maturano, M.; Saint-Aguet, P.; Roussel, L.; Duran, H.; Grima-Pettenati, J.
Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from Arabidopsis thaliana
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43
746-753
2005
Arabidopsis thaliana
brenda
Kawasaki, T.; Koita, H.; Nakatsubo, T.; Hasegawa, K.; Wakabayashi, K.; Takahashi, H.; Umemura, K.; Umezawa, T.; Shimamoto, K.
Cinnamoyl-CoA reductase, a key enzyme in lignin biosynthesis, is an effector of small GTPase Rac in defense signaling in rice
Proc. Natl. Acad. Sci. USA
103
230-235
2006
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brenda
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Characterization of a cinnamoyl-CoA reductase that is associated with stem development in wheat
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58
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Triticum aestivum (A8DNN6), Triticum aestivum
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Leple, J.C.; Dauwe, R.; Morreel, K.; Storme, V.; Lapierre, C.; Pollet, B.; Naumann, A.; Kang, K.Y.; Kim, H.; Ruel, K.; Lefebvre, A.; Joseleau, J.P.; Grima-Pettenati, J.; De Rycke, R.; Andersson-Gunneras, S.; Erban, A.; Fehrle, I.; Petit-Conil, M.; Kopka, J.; Polle, A.; Messens, E.; Sundberg, B.; Mans, M.a.n.s.f.
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19
3669-3691
2007
Populus trichocarpa (O65880)
brenda
Ralph, J.; Kim, H.; Lu, F.; Grabber, J.H.; Leple, J.C.; Berrio-Sierra, J.; Derikvand, M.M.; Jouanin, L.; Boerjan, W.; Lapierre, C.
Identification of the structure and origin of a thioacidolysis marker compound for ferulic acid incorporation into angiosperm lignins (and an indicator for cinnamoyl CoA reductase deficiency)
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53
368-379
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brenda
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Redirection of the phenylpropanoid pathway to feruloyl malate in Arabidopsis mutants deficient for cinnamoyl-CoA reductase 1
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227
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2008
Arabidopsis thaliana
brenda
Wadenbaeck, J.; von Arnold, S.; Egertsdotter, U.; Walter, M.H.; Grima-Pettenati, J.; Goffner, D.; Gellerstedt, G.; Gullion, T.; Clapham, D.
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17
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brenda
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185
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Panicum virgatum (D2IX40), Panicum virgatum (D2IX45), Panicum virgatum
brenda
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Isolation and characterization of a gene encoding cinnamoyl-CoA reductase from Isatis indigotica Fort.
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38
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Isatis tinctoria (D3J7Z3), Isatis tinctoria
brenda
Sonawane, P.; Patel, K.; Vishwakarma, R.K.; Singh, S.; Khan, B.M.
In silico mutagenesis and docking studies of active site residues suggest altered substrate specificity and possible physiological role of cinnamoyl CoA reductase 1 (Ll-CCRH1)
Bioinformation
9
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Leucaena leucocephala (Q08GL0), Leucaena leucocephala
brenda
Sonawane, P.; Vishwakarma, R.K.; Khan, B.M.
Biochemical characterization of recombinant cinnamoyl CoA reductase 1 (Ll-CCRH1) from Leucaena leucocephala
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58
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2013
Leucaena leucocephala
brenda
Sonawane, P.; Patel, K.; Vishwakarma, R.K.; Srivastava, S.; Singh, S.; Gaikwad, S.; Khan, B.M.
Probing the active site of cinnamoyl CoA reductase 1 (Ll-CCRH1) from Leucaena leucocephala
Int. J. Biol. Macromol.
60C
33-38
2013
Leucaena leucocephala (Q08GL0), Leucaena leucocephala
brenda
Tamasloukht, B.; Wong Quai Lam, M.S.; Martinez, Y.; Tozo, K.; Barbier, O.; Jourda, C.; Jauneau, A.; Borderies, G.; Balzergue, S.; Renou, J.P.; Huguet, S.; Martinant, J.P.; Tatout, C.; Lapierre, C.; Barriere, Y.; Goffner, D.; Pichon, M.
Characterization of a cinnamoyl-CoA reductase 1 (CCR1) mutant in maize: effects on lignification, fibre development, and global gene expression
J. Exp. Bot.
62
3837-3848
2011
Zea mays
brenda
Prasad, N.K.; Vindal, V.; Kumar, V.; Kabra, A.; Phogat, N.; Kumar, M.
Structural and docking studies of Leucaena leucocephala cinnamoyl CoA reductase
J. Mol. Model.
17
533-541
2011
Leucaena leucocephala (Q08GL0), Leucaena leucocephala
brenda
Prashant, S.; Sunita, M.; Sirisha, V.; Bhaskar, V.; Rao, A.; Narasu, M.; Kishor, P.
Isolation of cinnamoyl CoA reductase and cinnamyl alcohol dehydrogenase gene promoters from Leucaena leucocephala, a leguminous tree species, and characterization of tissue-specific activity in transgenic tobacco
Plant Cell
108
421-436
2012
Leucaena leucocephala
-
brenda
Wang, Z.; Cui, L.; Chen, C.; Liu, X.; Yan, Y.; Wang, Z.
Downregulation of cinnamoyl CoA reductase affects lignin and phenolic acids biosynthesis in Salvia miltiorrhiza Bunge
Plant Mol. Biol. Rep.
30
1229-1236
2012
Salvia miltiorrhiza (H9N7V9)
-
brenda
Zhou, R.; Jackson, L.; Shadle, G.; Nakashima, J.; Temple, S.; Chen, F.; Dixon, R.A.
Distinct cinnamoyl CoA reductases involved in parallel routes to lignin in Medicago truncatula
Proc. Natl. Acad. Sci. USA
107
17803-17808
2010
Medicago truncatula
brenda
Yeh, S.Y.; Huang, F.C.; Hoffmann, T.; Mayershofer, M.; Schwab, W.
FaPOD27 functions in the metabolism of polyphenols in strawberry fruit (Fragaria sp.)
Front. Plant Sci.
5
518
2014
Fragaria x ananassa (J7II91), Fragaria x ananassa
brenda
Sonawane, P.D.; Khan, B.M.; Gaikwad, S.M.
Conformational transitions of cinnamoyl CoA reductase 1 from Leucaena leucocephala
Int. J. Biol. Macromol.
64
30-35
2014
Leucaena leucocephala (Q08GL0), Leucaena leucocephala
brenda
Sonawane, P.; Vishwakarma, R.K.; Singh, S.; Gaikwad, S.; Khan, B.M.
Steady state fluorescence studies of wild type recombinant cinnamoyl CoA reductase (Ll-CCRH1) and its active site mutants
J. Fluoresc.
24
665-673
2014
Leucaena leucocephala (Q08GL0), Leucaena leucocephala
brenda
Khraiwesh, B.; Harb, J.; Qudeimat, E.
Molecular cloning and characterization of polygalacturonase-inhibiting protein and cinnamoyl-Coa reductase genes and their association with fruit storage conditions in blueberry (Vaccinium corymbosum)
J. Gen. Eng. Biotechnol.
11
1-8
2013
Vaccinium corymbosum (B6E2B5)
-
brenda
Han, B.; Liu, S.; Gai, Y.; Jiang, X.
Preparation of cinnamoyl-CoA and analysis of the enzyme activity of recombinant CCR protein from Populus tomentosa
J. Plant Biochem. Biotechnol.
23
348-357
2014
Populus tomentosa (Q6S3D7)
-
brenda
Ghosh, R.; Choi, B.; Kim, J.; Jeong, M.; Mohanta, T.; Bae, H.
Developmental- and stress-mediated expression analysis of cinnamoyl-CoA reductase 1 (CCR1) from Hibiscus cannabinus
J. Plant Interact.
10
158-166
2015
Hibiscus cannabinus (D9ZKR8), Hibiscus cannabinus C-9 (D9ZKR8)
-
brenda
Liu, S.; Qi, Q.; Chao, N.; Hou, J.; Rao, G.; Xie, J.; Lu, H.; Jiang, X.; Gai, Y.
Overexpression of artificially fused bifunctional enzyme 4CL1-CCR a method for production of secreted 4-hydroxycinnamaldehydes in Escherichia coli
Microb. Cell Fact.
14
118
2015
Populus tomentosa (B3VKV0)
brenda
Li, J.; Fan, F.; Wang, L.; Zhan, Q.; Wu, P.; Du, J.; Yang, X.; Liu, Y.
Cloning and expression analysis of cinnamoyl-CoA reductase (CCR) genes in sorghum
PeerJ
4
e2005
2016
Sorghum bicolor, Sorghum bicolor (C5XWV7), Sorghum bicolor (C5YLL4)
brenda
Srivastava, S.; Vishwakarma, R.K.; Arafat, Y.A.; Gupta, S.K.; Khan, B.M.
Abiotic stress induces change in cinnamoyl CoA reductase (CCR) protein abundance and lignin deposition in developing seedlings of Leucaena leucocephala
Physiol. Mol. Biol. Plants
21
197-205
2015
Leucaena leucocephala
brenda
Zhang, W.; Wei, R.; Chen, S.; Jiang, J.; Li, H.; Huang, H.; Yang, G.; Wang, S.; Wei, H.; Liu, G.
Functional characterization of CCR in birch (Betula platyphylla x Betula pendula) through overexpression and suppression analysis
Physiol. Plant.
154
283-296
2015
Betula platyphylla x Betula pendula (G3FJ91)
brenda
Pan, H.; Zhou, R.; Louie, G.V.; Muehlemann, J.K.; Bomati, E.K.; Bowman, M.E.; Dudareva, N.; Dixon, R.A.; Noel, J.P.; Wang, X.
Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis
Plant Cell
26
3709-3727
2014
Medicago truncatula, Medicago truncatula (G7JEE5), Petunia x hybrida (A0A059TC02), Petunia x hybrida
brenda
Xue, J.; Luo, D.; Xu, D.; Zeng, M.; Cui, X.; Li, L.; Huang, H.
CCR1, an enzyme required for lignin biosynthesis in Arabidopsis, mediates cell proliferation exit for leaf development
Plant J.
83
375-387
2015
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Sattler, S.A.; Walker, A.M.; Vermerris, W.; Sattler, S.E.; Kang, C.
Structural and biochemical characterization of cinnamoyl-CoA reductases
Plant Physiol.
173
1031-1044
2017
Sorghum bicolor (C5YLL4)
brenda
Chao, N.; Li, N.; Qi, Q.; Li, S.; Lv, T.; Jiang, X.N.; Gai, Y.
Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR
Planta
245
61-75
2017
Populus tomentosa (A0A0F7EVN0), Populus tomentosa (T1WWB5), Populus tomentosa
brenda
Van Acker, R.; Leple, J.C.; Aerts, D.; Storme, V.; Goeminne, G.; Ivens, B.; Legee, F.; Lapierre, C.; Piens, K.; Van Montagu, M.C.; Santoro, N.; Foster, C.E.; Ralph, J.; Soetaert, W.; Pilate, G.; Boerjan, W.
Improved saccharification and ethanol yield from field-grown transgenic poplar deficient in cinnamoyl-CoA reductase
Proc. Natl. Acad. Sci. USA
111
845-850
2014
Populus tremula x Populus alba
brenda
Ghosh, R.; Choi, B.; Cho, B.K.; Lim, H.S.; Park, S.U.; Bae, H.J.; Natarajan, S.; Bae, H.
Characterization of developmental- and stress-mediated expression of cinnamoyl-CoA reductase in kenaf (Hibiscus cannabinus L.)
ScientificWorldJournal
2014
601845
2014
Hibiscus cannabinus (A0A023HHB5), Hibiscus cannabinus (D9ZKR8), Hibiscus cannabinus
brenda
Ponniah, S.; Shang, Z.; Akbudak, M.; Srivastava, V.; Manoharan, M.
Down-regulation of hydroxycinnamoyl CoA shikimate hydroxycinnamoyl transferase, cinnamoyl CoA reductase, and cinnamyl alcohol dehydrogenase leads to lignin reduction in rice (Oryza sativa L. ssp. japonica cv. Nipponbare)
Plant Biotechnol. Rep.
11
17-27
2017
Oryza sativa Japonica Group (Q6K9A2)
-
brenda
Shi, C.; Qi, B.; Wang, X.; Shen, L.; Luo, J.; Zhang, Y.
Proteomic analysis of the key mechanism of exocarp russet pigmentation of semi-russet pear under rainwater condition
Sci. Hortic.
254
178-186
2019
Pyrus pyrifolia (F4Y9E7)
-
brenda
Smith, R.A.; Cass, C.L.; Mazaheri, M.; Sekhon, R.S.; Heckwolf, M.; Kaeppler, H.; de Leon, N.; Mansfield, S.D.; Kaeppler, S.M.; Sedbrook, J.C.; Karlen, S.D.; Ralph, J.
Suppression of cinnamoyl-CoA reductase increases the level of monolignol ferulates incorporated into maize lignins
Biotechnol. Biofuels
10
109
2017
Zea mays
brenda
Park, H.L.; Bhoo, S.H.; Kwon, M.; Lee, S.W.; Cho, M.H.
Biochemical and expression analyses of the rice cinnamoyl-CoA reductase gene family
Front. Plant Sci.
8
2099
2017
Oryza sativa Japonica Group
brenda
Yan, X.; Liu, J.; Kim, H.; Liu, B.; Huang, X.; Yang, Z.; Lin, Y.J.; Chen, H.; Yang, C.; Wang, J.P.; Muddiman, D.C.; Ralph, J.; Sederoff, R.R.; Li, Q.; Chiang, V.L.
CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa
New Phytol.
222
244-260
2019
Populus trichocarpa
brenda
Borah, P.; Khurana, J.P.
The OsFBK1 E3 ligase subunit affects anther and root secondary cell wall thickenings by mediating turnover of a cinnamoyl-CoA reductase
Plant Physiol.
176
2148-2165
2018
Oryza sativa
brenda
De Meester, B.; de Vries, L.; Oezparpucu, M.; Gierlinger, N.; Corneillie, S.; Pallidis, A.; Goeminne, G.; Morreel, K.; De Bruyne, M.; De Rycke, R.; Vanholme, R.; Boerjan, W.
Vessel-specific reintroduction of CINNAMOYL-COA REDUCTASE1 (CCR1) in dwarfed ccr1 mutants restores vessel and xylary fiber integrity and increases biomass
Plant Physiol.
176
611-633
2018
Arabidopsis thaliana
brenda
Chao, N.; Li, S.; Li, N.; Qi, Q.; Jiang, W.T.; Jiang, X.N.; Gai, Y.
Two distinct cinnamoyl-CoA reductases in Selaginella moellendorffii offer insight into the divergence of CCRs in plants
Planta
246
33-43
2017
Selaginella moellendorffii, Selaginella moellendorffii (A0A1V0HSA2)
brenda
Wang, Z.; Ge, Q.; Wang, Z.
Concerning the role of cinnamoyl CoA reductase gene in phenolic acids biosynthesis in Salvia miltiorrhiza
Russ. J. Plant Physiol.
64
553-559
2017
Salvia miltiorrhiza
-
brenda
Chao, N.; Jiang, W.T.; Wang, X.C.; Jiang, X.N.; Gai, Y.
Novel motif is capable of determining CCR and CCR-like proteins based on the divergence of CCRs in plants
Tree Physiol.
39
2019-2026
2019
Vitis vinifera, Pinus koraiensis, Oryza sativa Indica Group, Pinus massoniana, Ziziphus jujuba
brenda
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