Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

dihydromonacolin L acid,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)

dihydromonacolin L acid + O2 + [reduced NADPH---hemoprotein reductase] = monacolin L acid + [oxidized NADPH---hemoprotein reductase] + 2 H2O (overall reaction) [RN:R10793];
(1a) dihydromonacolin L acid + O2 + [reduced NADPH---hemoprotein reductase] = 3alpha-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R10791];
(1b) 3alpha-hydroxy-3,5-dihydromonacolin L acid = monacolin L acid + H2O (spontaneous) [RN:R10792]

R10791 R10792 R10793
Reaction

dihydromonacolin L acid [CPD:C20851];
O2 [CPD:C00007];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
3alpha-hydroxy-3,5-dihydromonacolin L acid [CPD:C20852]

A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3alpha-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].

EC 1.14.14.124 created 2014 as EC 1.14.13.197, transferred 2018 to EC 1.14.14.124

1  [PMID:2921224]

Treiber LR, Reamer RA, Rooney CS, Ramjit HG

Origin of monacolin L from Aspergillus terreus cultures.

J Antibiot (Tokyo) 42:30-6 (1989)
DOI:10.7164/antibiotics.42.30

2  [PMID:2276977]

Nakamura T, Komagata D, Murakawa S, Sakai K, Endo A

Isolation and biosynthesis of 3 alpha-hydroxy-3,5-dihydromonacolin L.

J Antibiot (Tokyo) 43:1597-600 (1990)
DOI:10.7164/antibiotics.43.1597

3  [PMID:21495633]

Barriuso J, Nguyen DT, Li JW, Roberts JN, MacNevin G, Chaytor JL, Marcus SL, Vederas JC, Ro DK

Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA.

J Am Chem Soc 133:8078-81 (2011)
DOI:10.1021/ja201138v

[ag:AAD34552]