1.14.14.126: beta-amyrin 28-monooxygenase

This is an abbreviated version!
For detailed information about beta-amyrin 28-monooxygenase, go to the full flat file.

Word Map on EC 1.14.14.126

1.14.14.126

triterpenoids

oleanolic

cyp716as

2,3-oxidosqualene

oleanane-type

lupeol

erythrodiol

sapogenins

oxidosqualene

hederagenin

amyrins

Reaction

+ 3 O2 + 3 [reduced NADPH-hemoprotein reductase] =

+ 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O

Synonyms

101251676, 101252702, alpha-amyrin 28-hydroxylase, amyrin C-28 oxidase, beta-amyrin 28-hydroxylase, beta-amyrin 28-oxidase, C-28 oxidase, CYP716A12, CYP716A140v2, CYP716A141, CYP716A15, CYP716A17, CYP716A175, CYP716A179, CYP716A244, CYP716A253, CYP716A254, CYP716A44, CYP716A46, CYP716A52v2, CYP716A94, EC 1.14.13.201, lupeol 28-hydroxylase, More, multifunctional oxidase, multifunctional P450, multifunctional triterpene C-28 oxidase, triterpene C-28 oxidase, triterpene monooxygenase

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.14.126 beta-amyrin 28-monooxygenase

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Results	in table
23	AA Sequence
16	Cloned(Commentary)
16	Cofactor
3	Expression
17	General Information
6	Localization
2	Metals/Ions
3	Molecular Weight [Da]
45	Natural Substrates/ Products (Substrates)
16	Organism
3	Pathway
2	pH Optimum
1	Protein Variants
8	Reaction
13	Reference
34	Source Tissue
71	Substrates and Products (Substrate)
4	Subunits
37	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]

Systematic Name

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Systematic Name on EC 1.14.14.126 - beta-amyrin 28-monooxygenase

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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.