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Your query returned 1 entry. Printable version
EC | 1.14.14.126 | ||||||
Accepted name: | β-amyrin 28-monooxygenase | ||||||
Reaction: | β-amyrin + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = oleanolate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction) (1a) β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = erythrodiol + [oxidized NADPH—hemoprotein reductase] + H2O (1b) erythrodiol + O2 + [reduced NADPH—hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O (1c) oleanolic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = oleanolate + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of β-amyrin, β-seco-amyrin, 11-oxo-β-amyrin and soysapogenol biosynthesis, click here | |||||||
Other name(s): | CYP716A52v2; CYP716A12; CYP16A75; β-amyrin 28-oxidase | ||||||
Systematic name: | β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (28-hydroxylating) | ||||||
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 α-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. | ||||||
Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc | ||||||
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