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(2E)-hexadec-2-enoyl-CoA + NADPH
palmitoyl-CoA + NADP+
-
-
-
-
?
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
2-methyl-trans-crotonyl-CoA + NADPH
2-methylbutanoyl-CoA + NADP+
-
2% of trans-crotonyl-CoA activity
-
-
?
2-trans,4-trans-decadienoyl-CoA + NADPH
?
-
low activity
-
-
?
2-trans,4-trans-hexadienoyl-CoA + NADPH
?
-
low activity
-
-
?
2-trans-8,11-eicosatrienoyl-CoA + NADPH
8,11-eicosadienoyl-CoA + NADP+
-
fat-free dietary elevates the activity
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
2-trans-octadecenoyl-CoA + NAD(P)H
octadecanoyl-CoA + NAD(P)+
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
2-trans-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
-
-
-
?
2-trans-tetradecenoyl-CoA + NADPH
tetradecanoyl-CoA + NADP+
3-butenoyl-CoA + NADPH
butanoyl-CoA + NADP+
-
7% of trans-crotonyl-CoA activity
-
-
?
3-methyl-crotonyl-CoA + NADPH
3-methylbutanoyl-CoA + NADP+
-
17% of trans-crotonyl-CoA activity
-
-
?
5-hydroxyundec-cis-2-enoyl-CoA + NADPH
5-hydroxyundecanoyl-CoA + NADP+
-
-
-
-
?
6,9-octadecadienoyl-CoA + NADPH
?
-
fat-free dietary elevates the activity
-
-
?
acetyl-CoA + NADPH + H+
?
-
-
-
-
r
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NADPH
butyryl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
additional information
?
-
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
-
-
-
?
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
-
-
?
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
-
-
-
?
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
substrate is not specified as cis- or trans-octenoyl-CoA
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
-
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
mitochondrial reductase II shows high activity, cofactor NADH
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
-
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
15% of trans-crotonyl-CoA activity
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
mitochondrial reductases II and III, low activity, cofactor NADH for isoform II and NADH or NADPH for isoform III
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
13% of trans-crotonyl-CoA activity
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
-
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
30% of trans-crotonyl-CoA activity
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
mitochondrial enzymes, reductase III shows highest activity, reductase I shows 45% activity of that with crotonyl-CoA, reductase II shows lower activity, cofactor NADH for isoform I and II and NADH or NADPH for isoform III
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
-
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
-
-
?
2-trans-octadecenoyl-CoA + NAD(P)H
octadecanoyl-CoA + NAD(P)+
-
cofactor NADH, mitochondrial reductase I shows 25% activity of that with crotonyl-CoA, reductase II shows highest activity
-
-
?
2-trans-octadecenoyl-CoA + NAD(P)H
octadecanoyl-CoA + NAD(P)+
-
i.e. 2-trans-oleoyl-CoA
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
-
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
-
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
mitochondrial enzyme, NADH-specific reaction
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
-
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
-
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
substrate is not specified as cis- or trans-octenoyl-CoA
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
trans isomer exhibits 1/3 of activity of cis isomer
-
-
?
2-trans-tetradecenoyl-CoA + NADPH
tetradecanoyl-CoA + NADP+
-
-
-
-
?
2-trans-tetradecenoyl-CoA + NADPH
tetradecanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
cis-crotonyl-CoA 30% of trans-crotonyl-CoA activity
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
mitochondrial reductase I, no specification of stereoisomer, cofactor NADH
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
enzyme is involved in synthesizing methylmalonyl-CoA precursors for monensin biosynthesis, pathway flux, overview
-
-
?
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
-
r
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
-
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
-
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme activity is higher in neurological Trembler mouse mutant than in wild-type
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
-
i.e. arachidoyl-CoA
?
additional information
?
-
-
no reduction of trans-crotonyl-S-pantetheine
-
-
?
additional information
?
-
-
no cis-isomeric substrates tested, classification is not definite
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
no activity with acetoacetyl-CoA or (R)-3-hydroxybutyryl-CoA
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
mitochondrial reductase III uses substrate with chain length of C4-C12
-
-
?
additional information
?
-
-
no cis-isomeric substrates tested, classification is not definite
-
-
?
additional information
?
-
-
active as part of fatty acid synthetase by incorporation of acetyl-CoA in mitochondria and of malonyl-CoA in cytosol
-
-
?
additional information
?
-
-
very slow reduction of substrate with chain length C4, C10, C12
-
-
?
additional information
?
-
-
FMN is essential for the reaction, tightly bound to apoprotein
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
optimal activity with chain length C10
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
specific for alpha/beta-unsaturated CoA derivatives with chain lengths of 4-16 C atoms, neither involved in beta-oxidation of fatty acids nor de novo-synthesis of fatty acids via malonyl-CoA
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-hexadec-2-enoyl-CoA + NADPH
palmitoyl-CoA + NADP+
-
-
-
-
?
5-hydroxyundec-cis-2-enoyl-CoA + NADPH
5-hydroxyundecanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
enzyme is involved in synthesizing methylmalonyl-CoA precursors for monensin biosynthesis, pathway flux, overview
-
-
?
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
additional information
?
-
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme activity is higher in neurological Trembler mouse mutant than in wild-type
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
active as part of fatty acid synthetase by incorporation of acetyl-CoA in mitochondria and of malonyl-CoA in cytosol
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
role in beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
specific for alpha/beta-unsaturated CoA derivatives with chain lengths of 4-16 C atoms, neither involved in beta-oxidation of fatty acids nor de novo-synthesis of fatty acids via malonyl-CoA
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Bernert, J.T.; Sprecher, H.
An analysis of partial reactions in the overall chain elongation of saturated and unsaturated fatty acids by rat liver microsomes
J. Biol. Chem.
252
6736-6744
1977
Rattus norvegicus
brenda
Bernert, J.T.; Sprecher, H.
The isolation of acyl-CoA derivatives as products of partial reactions in the microsomal chain elongation of fatty acids
Biochim. Biophys. Acta
573
436-442
1979
Rattus norvegicus
brenda
Prasad, M.R.; Chiang, C.F.; Cook, L.; Cinti, D.L.
Solubilization and purification of hepatic microsomal trans-2-enoyl-CoA reductase: evidence for the existence of a second long-chain enoyl-CoA reductase
Arch. Biochem. Biophys.
237
535-544
1985
Rattus norvegicus
brenda
Nagi, M.N.; Prasad, M.R.; Cook, L.; Cinti, D.
Biochemical properties of short- and long-chain rat liver microsomal trans-2-enoyl coenzyme A reductase
Arch. Biochem. Biophys.
226
50-64
1983
Rattus norvegicus
brenda
Prasad, M.R.; Nagi, M.N.; Cook, L.; Cinti, D.L.
Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase
Biochem. Biophys. Res. Commun.
113
659-665
1983
Rattus norvegicus
brenda
Cinti, D.L.; Nagi, M.N.; Cook, L.; White, R.E.
Evidence for a second microsomal trans-2-enoyl coenzyme A reductase in rat liver. NADPH-specific short chain reductase
J. Biol. Chem.
257
14333-14340
1982
Rattus norvegicus
brenda
Nagi, M.N.; Cook, L.; Ghesquier, D.; Cinti, D.L.
Site of inhibition of rat liver microsomal fatty acid chain elongation system by dec-2-ynoyl coenzyme A. Possible mechanism of inhibition
J. Biol. Chem.
261
13598-13605
1986
Rattus norvegicus
brenda
Nagi, M.N.; Cook, L.; Laguna, J.C.; Cinti, D.L.
Dual action of 2-decynoyl coenzyme A: inhibitor of hepatic mitochondrial trans-2-enoyl coenzyme A reductase and peroxisomal bifunctional protein and substrate for the mitochondrial beta-oxidation system
Arch. Biochem. Biophys.
267
1-12
1988
Rattus norvegicus
brenda
Laguna, J.C.; Nagi, M.; Cook, L.; Cinti, D.L.
Action of Ebselen on rat hepatic microsomal enzyme-catalyzed fatty acid chain elongation, desaturation, and drug biotransformation
Arch. Biochem. Biophys.
269
272-283
1989
Rattus norvegicus
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Fatty acid synthesis in mitochondria of Euglena gracilis
Eur. J. Biochem.
142
121-126
1984
Euglena gracilis
brenda
Kikuchi, S.; Kusaka, T.
Purification of NADPH-dependent enoyl-CoA reductase involved in the malonyl-CoA dependent fatty acid elongation system of Mycobacterium smegmatis
J. Biochem.
96
841-848
1984
Mycolicibacterium smegmatis
brenda
Strom, K.A.; Kumar, S.
Activation and inhibition of crotonyl-coenzyme A reductase activity of bovine mammary fatty acid synthetase
J. Biol. Chem.
254
8159-8162
1979
Bos taurus
-
brenda
Strom, K.A.; Galeos, W.L.; Davidson, L.A.; Kumar, S.
Enoyl coenzyme A reduction by bovine mammary fatty acid synthetase. Specificity and other characteristics
J. Biol. Chem.
254
8153-8158
1979
Bos taurus
brenda
Maitra, S.K.; Kumar, S.
Crotonyl coenzyme A reductase activity of bovine mammary fatty acid synthetase
J. Biol. Chem.
249
111-117
1974
Bos taurus
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