KEGG   ENZYME: 1.14.14.60
Entry
EC 1.14.14.60               Enzyme                                 
Name
ferruginol monooxygenase;
CYP76AH24;
CYP76AH3
Class
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
Sysname
ferruginol,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (11-hydroxyferruginol-forming)
Reaction(IUBMB)
ferruginol + [reduced NADPH---hemoprotein reductase] + O2 = 11-hydroxyferruginol + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R11951]
Reaction(KEGG)
R11951;
(other) R11988
Substrate
ferruginol [CPD:C09092];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
11-hydroxyferruginol [CPD:C21796];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A cytochrome P-450 (heme-thiolate) protein isolated from the plants Salvia pomifera (apple sage) and Salvia miltiorrhiza (danshen). 11-Hydroxyferruginol is a precursor of carnosic acid, a potent antioxidant.
History
EC 1.14.14.60 created 2018
Pathway
ec00904  Diterpenoid biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K22635  ferruginol monooxygenase / sugiol synthase
K22636  ferruginol synthase / ferruginol monooxygenase
Genes
SMIL131015109 131015114
Reference
1  [PMID:26976595]
  Authors
Ignea C, Athanasakoglou A, Ioannou E, Georgantea P, Trikka FA, Loupassaki S, Roussis V, Makris AM, Kampranis SC
  Title
Carnosic acid biosynthesis elucidated by a synthetic biology platform.
  Journal
Proc Natl Acad Sci U S A 113:3681-6 (2016)
DOI:10.1073/pnas.1523787113
  Sequence
Reference
2  [PMID:27703160]
  Authors
Scheler U, Brandt W, Porzel A, Rothe K, Manzano D, Bozic D, Papaefthimiou D, Balcke GU, Henning A, Lohse S, Marillonnet S, Kanellis AK, Ferrer A, Tissier A
  Title
Elucidation of the biosynthesis of carnosic acid and its reconstitution in yeast.
  Journal
Nat Commun 7:12942 (2016)
DOI:10.1038/ncomms12942
Reference
3  [PMID:26682704]
  Authors
Guo J, Ma X, Cai Y, Ma Y, Zhan Z, Zhou YJ, Liu W, Guan M, Yang J, Cui G, Kang L, Yang L, Shen Y, Tang J, Lin H, Ma X, Jin B, Liu Z, Peters RJ, Zhao ZK, Huang L
  Title
Cytochrome P450 promiscuity leads to a bifurcating biosynthetic pathway for tanshinones.
  Journal
New Phytol 210:525-34 (2016)
DOI:10.1111/nph.13790
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.60
IUBMB Enzyme Nomenclature: 1.14.14.60
ExPASy - ENZYME nomenclature database: 1.14.14.60
BRENDA, the Enzyme Database: 1.14.14.60
LinkDB

DBGET integrated database retrieval system