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Information on EC 1.14.14.126 - beta-amyrin 28-monooxygenase and Organism(s) Vitis vinifera and UniProt Accession F6H9N6

for references in articles please use BRENDA:EC1.14.14.126
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IUBMB 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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Vitis vinifera
UNIPROT: F6H9N6
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The taxonomic range for the selected organisms is: Vitis vinifera
The enzyme appears in selected viruses and cellular organisms
Synonyms
multifunctional p450, cyp716a12, multifunctional oxidase, cyp716a52v2, cyp716a179, cyp716a253, c-28 oxidase, triterpene c-28 oxidase, cyp716a244, cyp716a94, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP716A15
F1T282
-
CYP716A17
F1T283
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
erythrodiol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
erythrodiol + [reduced NADPH-hemoprotein reductase] + O2
oleanolic aldehyde + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
oleanolic aldehyde + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-amyrin + [reduced NADPH-hemoprotein reductase] + O2
ursolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
-
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
production of oleanolate in grape skin
-
-
?
lupeol + [reduced NADPH-hemoprotein reductase] + O2
betulinate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
lupane saponin biosynthesis in grape
-
-
?
beta-amyrin + [reduced NADPH-hemoprotein reductase] + O2
oleanolate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
F1T282, F1T283
production of oleanolate in grape skin
-
-
?
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
F1T282, F1T283
-
Manually annotated by BRENDA team
F1T282, F1T283
-
Manually annotated by BRENDA team
F1T282, F1T283
-
Manually annotated by BRENDA team
F1T282, F1T283
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C7A15_VITVI
480
1
54651
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression in Spodoptera frugiperda 9 insect cells and transgenic yeast
F1T282, F1T283
heterologous expression in Spodoptera frugiperda 9 insect cells and transgenic yeast
F1T282, F1T283
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
Medicago truncatula (Q2MJ20), Medicago truncatula, Vitis vinifera (F1T282), Vitis vinifera (F1T283), Vitis vinifera
Manually annotated by BRENDA team