The Enzyme Database

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EC 1.14.13.201      
Transferred entry: β-amyrin 28-monooxygenase. Now EC 1.14.14.126, β-amyrin 28-monooxygenase
[EC 1.14.13.201 created 2015, deleted 2018]
 
 
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
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, KEGG, MetaCyc
References:
1.  Fukushima, E.O., Seki, H., Ohyama, K., Ono, E., Umemoto, N., Mizutani, M., Saito, K. and Muranaka, T. CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis. Plant Cell Physiol. 52 (2011) 2050–2061. [DOI] [PMID: 22039103]
2.  Han, J.Y., Kim, M.J., Ban, Y.W., Hwang, H.S. and Choi, Y.E. The involvement of β-amyrin 28-oxidase (CYP716A52v2) in oleanane-type ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol. 54 (2013) 2034–2046. [DOI] [PMID: 24092881]
3.  Moses, T., Pollier, J., Faizal, A., Apers, S., Pieters, L., Thevelein, J.M., Geelen, D. and Goossens, A. Unraveling the triterpenoid saponin biosynthesis of the African shrub Maesa lanceolata. Mol. Plant 8 (2015) 122–135. [DOI] [PMID: 25578277]
[EC 1.14.14.126 created 2015 as EC 1.14.13.201, transferred 2018 to EC 1.14.14.126]
 
 
EC 2.4.1.368     
Accepted name: oleanolate 3-O-glucosyltransferase
Reaction: UDP-α-D-glucose + oleanolate = UDP + oleanolate 3-O-β-D-glucoside
Glossary: oleanolate = 3β-hydroxyolean-12-en-28-oate
Other name(s): UGT73C10 (gene name); UGT73C11 (gene name)
Systematic name: UDP-α-D-glucose:oleanolate 3-O-glucosyltransferase
Comments: The enzyme has been characterized from the saponin-producing crucifer plant Barbarea vulgaris.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Augustin, J.M., Drok, S., Shinoda, T., Sanmiya, K., Nielsen, J.K., Khakimov, B., Olsen, C.E., Hansen, E.H., Kuzina, V., Ekstrom, C.T., Hauser, T. and Bak, S. UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris catalyze sapogenin 3-O-glucosylation in saponin-mediated insect resistance. Plant Physiol. 160 (2012) 1881–1895. [PMID: 23027665]
[EC 2.4.1.368 created 2019]
 
 


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