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Information on EC 1.14.14.126 - beta-amyrin 28-monooxygenase
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1.14.14.126 beta-amyrin 28-monooxygenaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro. The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert alpha-amyrin and lupeol to ursolic acid and betulinic acid, respectively. The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyse the reaction to completion, resulting in accumulation of both intermediates.
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Word Map
- 1.14.14.126
-
triterpenoids
-
oleanolic
-
cyp716as
- 2,3-oxidosqualene
-
oleanane-type
- lupeol
- erythrodiol
-
sapogenins
- oxidosqualene
-
hederagenin
-
amyrins
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
multifunctional p450, cyp716a12, multifunctional oxidase, cyp716a52v2, cyp716a179, cyp716a253, c-28 oxidase, triterpene c-28 oxidase, cyp716a244, cyp716a94, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-amyrin 28-oxidase
CYP716A12
CYP716A179
EC 1.14.13.201
-
-
formerly
-
triterpene C-28 oxidase
additional information
additional information
cf. EC 1.14.13.173, beta-amyrin C-16beta oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-amyrin + 3 O2 + 3 [reduced NADPH-hemoprotein reductase] = oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
beta-amyrin + O2 + [reduced NADPH-hemoprotein reductase] = erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
erythrodiol + O2 + [reduced NADPH-hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
oleanolic aldehyde + O2 + [reduced NADPH-hemoprotein reductase] = oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + 3 O2 + 3 [reduced NADPH-hemoprotein reductase] = oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
-
beta-amyrin + 3 O2 + 3 [reduced NADPH-hemoprotein reductase] = oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
beta-amyrin + O2 + [reduced NADPH-hemoprotein reductase] = erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
beta-amyrin + O2 + [reduced NADPH-hemoprotein reductase] = erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
erythrodiol + O2 + [reduced NADPH-hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(1b)
-
-
-
erythrodiol + O2 + [reduced NADPH-hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(1b)
oleanolic aldehyde + O2 + [reduced NADPH-hemoprotein reductase] = oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
(1c)
-
-
-
oleanolic aldehyde + O2 + [reduced NADPH-hemoprotein reductase] = oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
(1c)
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SYSTEMATIC NAME
IUBMB Comments
beta-amyrin,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (28-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro. The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert alpha-amyrin and lupeol to ursolic acid and betulinic acid, respectively. The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyse the reaction to completion, resulting in accumulation of both intermediates.
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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
alpha-amyrin + 3 O2 + 3 NADPH + 3 H+
ursolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
maniladiol + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-16beta
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-28
-
-
?
betulin + [reduced NADPH-hemoprotein reductase] + O2
betulinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
betulinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
betulinic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
germanicol + 3 O2 + 3 NADPH + 3 H+
morolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
lupeol + 3 O2 + 3 NADPH + 3 H+
betulinate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
lupeol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
betulin + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
lupeol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
betulinic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
maniladiol + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
oleanolic acid + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-16beta, reaction of EC 1.14.13.173
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
ursolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
ursolic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
uvaol + [reduced NADPH-hemoprotein reductase] + O2
ursolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
Glycyrrhiza uralensis 308-19
overall reaction
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
oleanolate + 3 NADP+ + 4 H2O
-
-
-
?
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
oleanolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
oleanolate + 3 NADP+ + 4 H2O
-
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + O2 + NADPH + H+
erythrodiol + NADP+ + H2O
-
-
-
?
beta-amyrin + O2 + NADPH + H+
erythrodiol + NADP+ + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
F8J4R7
overall reaction
CYP716A12 mainly catalyzes the sequential three-step oxidation at the C-28 position necessary to transform beta-amyrin into oleanolic acid
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
the enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
production of oleanolate in grape skin
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
F8J4R7
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
lupane saponin biosynthesis in grape
-
-
?
maniladiol + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
maniladiol + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-28
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
additional information
?
-
metabolite identification by mass spectrometry
-
-
?
additional information
?
-
-
metabolite identification by mass spectrometry
-
-
?
additional information
?
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
-
-
?
additional information
?
-
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
-
-
?
additional information
?
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol. The enzyme is a multifunctional oxidase enzymes with beta-amyrin 28-hydroxylase, alpha-amyrin 28-hydroxylase, and lupeol 28-hydroxylase activities
-
-
?
additional information
?
-
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol. The enzyme is a multifunctional oxidase enzymes with beta-amyrin 28-hydroxylase, alpha-amyrin 28-hydroxylase, and lupeol 28-hydroxylase activities
-
-
?
additional information
?
-
the enzyme catalyzes a three-step oxidation reaction at the C-28 position of beta-amyrin, alpha-amyrin, and lupeol to produce oleanolic acid, ursolic acid, and betulinic acid, respectively
-
-
?
additional information
?
-
-
the enzyme catalyzes a three-step oxidation reaction at the C-28 position of beta-amyrin, alpha-amyrin, and lupeol to produce oleanolic acid, ursolic acid, and betulinic acid, respectively
-
-
?
additional information
?
-
Glycyrrhiza uralensis 308-19
the enzyme catalyzes a three-step oxidation reaction at the C-28 position of beta-amyrin, alpha-amyrin, and lupeol to produce oleanolic acid, ursolic acid, and betulinic acid, respectively
-
-
?
additional information
?
-
EB148173
CYP716A175 catalyses the C-28 oxidation of alpha-amyrin, beta-amyrin, lupeol and germanicol, producing ursolic acid, oleanolic acid, betulinic acid, and putatively morolic acid. CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position
-
-
?
additional information
?
-
-
CYP716A175 catalyses the C-28 oxidation of alpha-amyrin, beta-amyrin, lupeol and germanicol, producing ursolic acid, oleanolic acid, betulinic acid, and putatively morolic acid. CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position
-
-
?
additional information
?
-
EB148173
CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position. CYP716A175 has a similar oxidizing capacity for the triterpene scaffold alpha-amyrin, beta-amyrin, and lupeol but not for germanicol
-
-
?
additional information
?
-
-
CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position. CYP716A175 has a similar oxidizing capacity for the triterpene scaffold alpha-amyrin, beta-amyrin, and lupeol but not for germanicol
-
-
?
additional information
?
-
CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry
-
-
?
additional information
?
-
CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry
-
-
?
additional information
?
-
-
CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry
-
-
?
additional information
?
-
hydroxylation of beta-amyrin at C-16beta is the main activity of enzyme CYP716A141, but CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry. The enzyme hydroxylates oleanolic acid, beta-amyrin, and maniladiol
-
-
?
additional information
?
-
hydroxylation of beta-amyrin at C-16beta is the main activity of enzyme CYP716A141, but CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry. The enzyme hydroxylates oleanolic acid, beta-amyrin, and maniladiol
-
-
?
additional information
?
-
-
hydroxylation of beta-amyrin at C-16beta is the main activity of enzyme CYP716A141, but CYP716A141 is capable of catalyzing oxidation at both C-16beta and C-28, metabolites analysis by mass spectrometry. The enzyme hydroxylates oleanolic acid, beta-amyrin, and maniladiol
-
-
?
additional information
?
-
the enzyme produces erythrodiol and oleanolic acid as C-28 oxidation products of beta-amyrin
-
-
?
additional information
?
-
the enzyme produces erythrodiol and oleanolic acid as C-28 oxidation products of beta-amyrin
-
-
?
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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
alpha-amyrin + 3 O2 + 3 NADPH + 3 H+
ursolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
beta-amyrin + O2 + NADPH + H+
erythrodiol + NADP+ + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
maniladiol + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-16beta
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-28
-
-
?
betulin + [reduced NADPH-hemoprotein reductase] + O2
betulinic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
betulinic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
betulinic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
germanicol + 3 O2 + 3 NADPH + 3 H+
morolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
lupeol + 3 O2 + 3 NADPH + 3 H+
betulinate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
lupeol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
betulin + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
-
-
-
?
lupeol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
betulinic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
maniladiol + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-28
-
-
?
oleanolic acid + [reduced NADPH-hemoprotein reductase] + O2
cochalic acid + [oxidized NADPH-hemoprotein reductase] + H2O
hydroxylation at C-16beta, reaction of EC 1.14.13.173
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
ursolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
ursolic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
uvaol + [reduced NADPH-hemoprotein reductase] + O2
ursolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
alpha-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
ursolic acid + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
Glycyrrhiza uralensis 308-19
overall reaction
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
uvaol + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
oleanolate + 3 NADP+ + 4 H2O
EB148173
overall reaction
-
-
?
beta-amyrin + 3 O2 + 3 NADPH + 3 H+
oleanolate + 3 NADP+ + 4 H2O
-
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + 3 [reduced NADPH-hemoprotein reductase] + 3 O2
oleanolate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
overall reaction
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
the enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
production of oleanolate in grape skin
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
F1T282, F1T283
lupane saponin biosynthesis in grape
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
Glycyrrhiza uralensis 308-19
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
-
-
?
additional information
?
-
-
CYP716A244 is a beta-amyrin 28-oxidase that converts beta-amyrin into oleanolic acid via formation of erythrodiol
-
-
?
additional information
?
-
EB148173
CYP716A175 catalyses the C-28 oxidation of alpha-amyrin, beta-amyrin, lupeol and germanicol, producing ursolic acid, oleanolic acid, betulinic acid, and putatively morolic acid. CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position
-
-
?
additional information
?
-
-
CYP716A175 catalyses the C-28 oxidation of alpha-amyrin, beta-amyrin, lupeol and germanicol, producing ursolic acid, oleanolic acid, betulinic acid, and putatively morolic acid. CYP716A175 catalyses the three-step oxidation of triterpene backbones at the C-28 position
-
-
?
additional information
?
-
the enzyme produces erythrodiol and oleanolic acid as C-28 oxidation products of beta-amyrin
-
-
?
additional information
?
-
the enzyme produces erythrodiol and oleanolic acid as C-28 oxidation products of beta-amyrin
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from Tonggubao Village, Machi Town, Changyang County, Hubei Province of China in May of 2014
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
exclusive expresion of CYP716A46 in flowers
brenda
F8J4R7
significant increase in expression is observed in the reproductive stages, with a maximum expression at flowering
brenda
the enzyme is highly expressed in roots
brenda
additional information
transcript level of CYP716A179 in leaves is lower than that in intact roots
brenda
additional information
-
transcript level of CYP716A179 in leaves is lower than that in intact roots
brenda
additional information
Glycyrrhiza uralensis 308-19
-
transcript level of CYP716A179 in leaves is lower than that in intact roots
-
brenda
additional information
EB148173
gene expression pattern analysis of CYP716A175 in 20 apple cultivars
brenda
additional information
-
gene expression pattern analysis of CYP716A175 in 20 apple cultivars
brenda
additional information
F8J4R7
expression of the gene occurs in all the organs and the developmental stages
brenda
additional information
-
expression of the gene occurs in all the organs and the developmental stages
brenda
additional information
spatiotemporal expression patterns of amyrin synthases and amyrin C-28 oxidases
brenda
additional information
-
spatiotemporal expression patterns of amyrin synthases and amyrin C-28 oxidases
brenda
additional information
very low levels of mRNA in other organs than rhizome
brenda
additional information
-
very low levels of mRNA in other organs than rhizome
brenda
additional information
transcriptome analysis in different tissues using RNA sequencing technology, overview
brenda
additional information
transcriptome analysis in different tissues using RNA sequencing technology, overview
brenda
additional information
-
transcriptome analysis in different tissues using RNA sequencing technology, overview
brenda
additional information
no enzyme expression in leaves, roots, and stems
brenda
additional information
no enzyme expression in leaves, roots, and stems
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzyme belongs to the CYP716A subfamily of cytochrome P450 monooxygenases
evolution
EB148173
CYP716A175 is clearly grouped with the CYP716A subfamily. Expression patterns of triterpene-related genes in different apple cultivars, overview
evolution
the enzyme belongs to the CYP716C subfamily, many CYP716 family P450 enzymes are characterized as multifunctional triterpene C-28 oxidases, which oxidize alpha-amyrin and beta-amyrin to the widely distributed triterpenoids ursolic and oleanolic acids, respectively. Isolation of all six CYP716 family genes from tomato, including CYP716A46, and sequence comparisons
evolution
the enzyme belongs to the CYP716C subfamily, many CYP716 family P450 enzymes are characterized as multifunctional triterpene C-28 oxidases, which oxidize alpha-amyrin and beta-amyrin to the widely distributed triterpenoids ursolic and oleanolic acids, respectively. Isolation of all six CYP716 family genes from tomato, including gene CYP716A44, and sequence comparisons
metabolism
the enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro
metabolism
cytochrome P450 monooxygenase CYP716A254 is involved in oleanane-type triterpenoid saponins biosynthesis, i.e. the biosynthesis of oleanolic acid, which involves cyclization of 2,3-oxidosqualene to the oleanane-type triterpenoid skeleton, followed by a series of oxidation reactions catalyzed by cytochrome P450 monooxygenase (CYP450), Proposed biosynthetic pathway for oleanolic acid in Anemone flaccida, overview
metabolism
enzymes CYP716A252 and CYP716A253 catalyze sequential three-step oxidation at the C-28 position of alpha-amyrin and beta-amyrin to produce ursolic acid and oleanolic acid, respectively, essential roles for both of these CYP716As in constitutive biosynthesis of ursolic acid and oleanolic acid in sweet basil leaves, similar as well as distinct roles of CYP716A252 and CYP716A253 for the spatio-temporal biosynthesis of pentacyclic triterpenes. The cyclization of 2,3-oxidosqualene into either of two structural isomers, alpha-amyrin or beta-amyrin is the initial diversifying step for ursolic acid and oleanolic acid biosynthesis, pathway overview
metabolism
the enzyme catalyzes a step in the putative saponin biosynthetic pathway from 2,3-oxidosqualene to hederagenin saponin, overview. Two enzymes (beta-amyrin synthase and beta-amyrin 28-oxidase) are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
metabolism
oleanane-type triterpenes are the major saponin components in Eleutherococcus senticosus. The two enzymes, beta-amyrin synthase and beta-amyrin 28-oxidase, are essential for oleanane-type saponin biosynthesis from 2,3-oxidosqualene
metabolism
the enzyme is involved in the triterpenoid biosynthesis in tomato
physiological function
F8J4R7
enzyme is responsible for an early step in the saponin biosynthetic pathway. Mutants in CYP716A12 are unable to produce hemolytic saponins and only synthetize soyasaponins. CYP716A12 catalyzes the oxidation of beta-amyrin and erythrodiol at the C-28 position, yielding oleanolic acid
physiological function
CYP716A140v2, catalyzed a three-step oxidation reaction at C-28 on beta-amyrin to produce oleanolic acid, a reaction performed by CYP716A subfamily P450s in a variety of plant species
physiological function
CYP716A244 is a beta-amyrin 28-oxidase involved in saponin biosynthesis, beta-amyrin is the oleanane-type triterpene backbone. beta-Amyrin is oxidised at the C-28 position in a sequential three-step oxidation by the single cytochrome P450 enzyme to yield oleanolic acid through erythrodiol
physiological function
CYP716A94 is a beta-amyrin 28-oxidase for the production of oleanolic acid
physiological function
cytochrome P450 monooxygenase CYP716A254 catalyzes the formation of oleanolic acid from beta-amyrin during oleanane-type triterpenoid saponins biosynthesis. Oleanolic acid is natural triterpenoid in plants with diverse biological activities
physiological function
the medicinal plant sweet basil (Ocimum basilicum) accumulates bioactive ursane- and oleanane-type pentacyclic triterpenes (PCTs), ursolic acid and oleanolic acid, respectively, in a spatio-temporal manner. Major role for CYP716A253 and a minor role for CYP716A252 in determining elicitor-induced biosynthesis of ursolic acid and oleanolic acid
additional information
enzyme CYP716A253 contains conserved amino acid motifs characteristic of bona fide CYP450s includig the highly conserved heme-binding motif FxxGxRxCxG at the C-terminal end, an EXXR.-.R motif (ERR triad) that maintains protein tertiary structure and positioning of the heme pocket, an A/GGXD/ET motif that participates in oxygen binding and activation, and a proline-rich and a hydrophobic regions at the N-terminal end
additional information
-
enzyme CYP716A253 contains conserved amino acid motifs characteristic of bona fide CYP450s includig the highly conserved heme-binding motif FxxGxRxCxG at the C-terminal end, an EXXR.-.R motif (ERR triad) that maintains protein tertiary structure and positioning of the heme pocket, an A/GGXD/ET motif that participates in oxygen binding and activation, and a proline-rich and a hydrophobic regions at the N-terminal end
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). C7A12_MEDTR
479
1
54713
Swiss-Prot
Secretory Pathway (Reliability: 1)
C7A15_VITVI
480
1
54651
Swiss-Prot
Secretory Pathway (Reliability: 1)
C7A17_VITVI
480
1
54637
Swiss-Prot
Secretory Pathway (Reliability: 2)
C7A44_SOLLC
476
1
54258
Swiss-Prot
Secretory Pathway (Reliability: 1)
C7A46_SOLLC
482
1
54862
Swiss-Prot
Secretory Pathway (Reliability: 1)
C7A52_PANGI
481
1
53955
Swiss-Prot
Secretory Pathway (Reliability: 1)
C7A81_BARVU
475
1
54966
Swiss-Prot
Secretory Pathway (Reliability: 2)
C7A94_KALSE
481
1
54011
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A5B6ZNP3_DAVIN
478
1
53977
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7A0T0_DAVIN
130
0
14961
TrEMBL
other Location (Reliability: 3)
A0A5B7ADD7_DAVIN
476
1
54091
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7ABB9_DAVIN
476
1
54114
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5B7AHZ6_DAVIN
131
0
14918
TrEMBL
other Location (Reliability: 3)
A0A5B6ZM05_DAVIN
271
1
30641
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZXJ9_DAVIN
218
0
24825
TrEMBL
other Location (Reliability: 2)
A0A5B7A378_DAVIN
217
0
23760
TrEMBL
Secretory Pathway (Reliability: 4)
A0A5B6ZLM3_DAVIN
389
1
43395
TrEMBL
other Location (Reliability: 3)
A0A5B6ZPA8_DAVIN
540
2
60806
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
virus-induced gene silencing (VIGS) in Ocimum basilicum, plasmids are individually transformed into Agrobacterium tumefaciens strain GV3101 by the freeze-thaw method
additional information
-
virus-induced gene silencing (VIGS) in Ocimum basilicum, plasmids are individually transformed into Agrobacterium tumefaciens strain GV3101 by the freeze-thaw method
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of PNY1 and CYP716A52v2 in yeast. Transgenic Panax ginseng plants constitutively overexpressing CYP716A52v2 and expressing a CYP716A52v2-RNAi are generated using Agrobacterium tumefaciens mediated genetic transformation
CYP716A244, DNA and amino acid sequence determination and analysis, phylogenetic analysis. quantitative RT-PCR enzyme expression analysis, transcriptomics analysis of plant leaves, recombinant expression in Saccharomyces cerevisiae, recombinant expression in trangsgenic Nicotiana tabacum, co-expression with beta-amyrin synthase, EsBAS
expression in Saccharomyces cerevisiae
gene CYP716A140v2, DNA and amino acid sequence determination and analysis, phylogenetic tree, quantitative real-time PCR enzyme expression analysis, recombinant coexpression of genes CYP716A140v2 and CYP716A141 in Saccharomyces cerevisiae strain 10, that shows increased cochalic acid levels
gene CYP716A141, DNA and amino acid sequence determination and analysis, phylogenetic tree, quantitative real-time PCR enzyme expression analysis, recombinant coexpression of genes CYP716A140v2 and CYP716A141 in Saccharomyces cerevisiae strain 10, that shows increased cochalic acid levels
gene CYP716A175, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR expression analysis, transient recombinant expression in Nicotiana benthamiana using the transformation method via Agrobacterium tumefaciens strain GV3101. The higher oxidizing efficiency of CYP716A175 for lupeol and beta-amyrin compared with germanicol preferentially drives the whole reaction chain to the production of betulinate and oleanolate rather than morolic acid. Transient expression in Saccharomyces cerevisiae shows the presence of the intermediate erythrodiol in addition to oleanolate, but not of oleanolic aldehyde. Sequential three-step oxidation reaction leading to oleanolate, low efficiency of CYP716A75 to oxidize erythrodiol in yeast
EB148173
gene CYP716A179, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative real-time PCR enzyme analysis, recombinant expression in Saccharomyces cerevisiae results in production of oleanolic acid, ursolic acid, and betulinic acid from beta-amyrin, alpha-amyrin, and lupeol, respectively, galactose-inducible dual expression of Lotus japonicus CPR1 and CYP716A179
gene CYP716A244, phylogenetic tree, quantitative real-time PCR expression analysis, transient recombinant expression in Nicotiana benthamiana using the transformation method via Agrobacterium tumefaciens strain GV3101, and transient recombinant expression in Saccharomyces cerevisiae with coexpression of Arabidopsis thaliana NADPH-CYP reductase
gene CYP716A253, semi-quantitative and quantitative RT-PCR enzyme expressison analysis, phylogenetic analysis, recombinant expression in Saccharomyces cerevisiae strain BY4741
gene CYP716A254, DNA and amino acid sequence determination and analysis, phylogenetic tree, heterologous expression in Saccharomyces cerevisiae strain WAT11 results in oxidation of beta-amyrin at the C-28 position to oleanolic acid production
gene CYP716A44, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, in beta-amyrin synthase (EC 5.4.99.39) and CYP716A44 co-expressing Saccharomyces cerevisiae strains SY57 and SY66 erythrodiol and oleanolic acid are detected as C-28 oxidation product of beta-amyrin
gene CYP716A46, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, in beta-amyrin synthase (EC 5.4.99.39) and CYP716A46 co-expressing Saccharomyces cerevisiae strains SY57 and SY66, erythrodiol and oleanolic acid are detected as C-28 oxidation product of beta-amyrin
gene CYP716A94, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Saccharomyces cerevisiae strain WAT21 microsomes, coexpression with Arabidopsis thaliana NADPH-CYP reductase leads to production of oleanolic acid, mass spectrometric analysis
heterologous expression in Spodoptera frugiperda 9 insect cells and transgenic yeast
heterologous expression in Spodoptera frugiperda 9 insect cells and transgenic yeast
heterologous expression in Spodoptera frugiperda 9 insect cells and transgenic yeast
F1T282, F1T283
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP716A52v2 mRNA does not respond to methyl jasmonate treatment during the entire culture period
infection with Sclerotinia sclerotiorum and treatement with methyljasmonate and ACC induce the enzyme up to 6.8, 4.3 and 91fold
methyl jasmonate treatment highly enhances CYP716A244 transcription at 12 h after methyl jasmonate treatment, and this enhancement declines as the culture time proceeds
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukushima, E.O., Seki, H.; Ohyama, K.; Ono, E.; Umemoto, N.; Mizutani, M.; Saito, K.; Muranaka, T.
CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis
Plant Cell Physiol.
52
2050-2061
2011
Vitis vinifera (F1T282), Vitis vinifera (F1T283), Vitis vinifera, Medicago truncatula (Q2MJ20), Medicago truncatula
brenda
Han, J.; Kim, M.; Ban, Y.; Hwang, H.; Choi, Y.
The involvement of beta-amyrin 28-oxidase (Cyp716a52v2) in oleanane-type ginsenoside biosynthesis in Panax ginseng
Plant Cell Physiol.
54
2034-2046
2013
Panax ginseng (I7C6E8), Panax ginseng
brenda
Carelli, M.; Biazzi, E.; Panara, F.; Tava, A.; Scaramelli, L.; Porceddu, A.; Graham, N.; Odoardi, M.; Piano, E.; Arcioni, S.; May, S.; Scotti, C.; Calderini, O.
Medicago truncatula CYP716A12 is a multifunctional oxidase involved in the biosynthesis of hemolytic saponins
Plant Cell
23
3070-3081
2011
Medicago truncatula (F8J4R7), Medicago truncatula
brenda
Zhan, C.; Ahmed, S.; Hu, S.; Dong, S.; Cai, Q.; Yang, T.; Wang, X.; Li, X.; Hu, X.
Cytochrome P450 CYP716A254 catalyzes the formation of oleanolic acid from beta-amyrin during oleanane-type triterpenoid saponins biosynthesis in Anemone flaccida
Biochem. Biophys. Res. Commun.
495
1271-1277
2018
Anemone flaccida (I7C6E8), Anemone flaccida
brenda
Yasumoto, S.; Seki, H.; Shimizu, Y.; Fukushima, E.O.; Muranaka, T.
Functional characterization of CYP716 family P450 enzymes in triterpenoid biosynthesis in tomato
Front. Plant Sci.
8
21
2017
Solanum lycopersicum (A0A3Q7HBJ5), Solanum lycopersicum (K4CEE8)
brenda
Misra, R.; Sharma, S.; Sandeep, S.; Garg, A.; Chanotiya, C.; Ghosh, S.
Two CYP716A subfamily cytochrome P450 monooxygenases of sweet basil play similar but nonredundant roles in ursane- and oleanane-type pentacyclic triterpene biosynthesis
New Phytol.
214
706-720
2017
Ocimum basilicum (A0A161ABB0), Ocimum basilicum
brenda
Jo, H.J.; Han, J.Y.; Hwang, H.S.; Choi, Y.E.
beta-Amyrin synthase (EsBAS) and beta-amyrin 28-oxidase (CYP716A244) in oleanane-type triterpene saponin biosynthesis in Eleutherococcus senticosus
Phytochemistry
135
53-63
2017
Eleutherococcus senticosus (A0A1P8W705), Eleutherococcus senticosus
brenda
Tamura, K.; Teranishi, Y.; Ueda, S.; Suzuki, H.; Kawano, N.; Yoshimatsu, K.; Saito, K.; Kawahara, N.; Muranaka, T.; Seki, H.
Cytochrome P450 monooxygenase CYP716A141 is a unique beta-amyrin C-16beta oxidase involved in triterpenoid saponin biosynthesis in Platycodon grandiflorus
Plant Cell Physiol.
58
874-884
2017
Platycodon grandiflorus (A0A1I9Q5Z0), Platycodon grandiflorus (A0A1V1FHP8), Platycodon grandiflorus
brenda
Han, J.Y.; Chun, J.H.; O, S.A.; Park, S.B.; Hwang, H.S.; Lee, H.; Choi, Y.E.
Transcriptomic analysis of Kalopanax septemlobus and characterization of KsBAS, CYP716A94, and CYP72A397 genes involved in hederagenin saponin biosynthesis
Plant Cell Physiol.
59
319-330
2017
Kalopanax septemlobus (A0A0S2II38), Kalopanax septemlobus
brenda
Tamura, K.; Seki, H.; Suzuki, H.; Kojoma, M.; Saito, K.; Muranaka, T.
CYP716A179 functions as a triterpene C-28 oxidase in tissue-cultured stolons of Glycyrrhiza uralensis
Plant Cell Rep.
36
437-445
2017
Glycyrrhiza uralensis (A0A1L7NXK5), Glycyrrhiza uralensis, Glycyrrhiza uralensis 308-19 (A0A1L7NXK5)
brenda
Andre, C.; Legay, S.; Deleruelle, A.; Nieuwenhuizen, N.; Punter, M.; Brendolise, C.; Cooney, J.; Lateur, M.; Hausman, J.; Larondelle, Y.; Laing, W.
Multifunctional oxidosqualene cyclases and cytochrome P450 involved in the biosynthesis of apple fruit triterpenic acids
New Phytol.
211
1279-1294
2016
Malus domestica (EB148173), Malus domestica
brenda
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Release 2023.1 (January 2023)
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