Information on EC 1.14.14.60 - ferruginol monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.60
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RECOMMENDED NAME
GeneOntology No.
ferruginol monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ferruginol + [reduced NADPH-hemoprotein reductase] + O2 = 11-hydroxyferruginol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carnosate bioynthesis
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Diterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
ferruginol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (11-hydroxyferruginol forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
cytochrome CYP76AH3 oxidizes ferruginol at two different carbon centers, and CYP76AK1 hydroxylates at C-20 of two of the resulting intermediates. Together, they convert ferruginol into 11,20-dihydroxy ferruginol and 11,20-dihydroxy sugiol en route to tanshinones. Silencing of CYP76AH3 leads to significant reduction in concentration of 11-hydroxyferruginol and 11-hydroxysugiol
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferruginol + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxyferruginol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
sugiol + [reduced NADPH-hemoprotein reductase] + O2
11-hydroxysugiol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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additional information
?
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enzyme additionally oxidizes at C-7 to yield sugiol, reaction of EC 1.14.14.65
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression is more abundant in the root than in aerial tissues
Manually annotated by BRENDA team
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glandular trichome
Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression Saccaromyces cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F112L
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mutant catalyzes ferruginol production in yeast 2 times more efficiently than the wild-type enzyme, while production of 11-hydroxy-ferruginol is abolished. mutant does not oxidize miltiradiene, reaction of EC 1.14.13.190, or manoyl oxide
V296L
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mutant produces 1.5 times more ferruginol, but 8fold less 11-hydroxy-ferruginol and 20fold less 11beta-hydroxy-manoyl oxide than the wild-type enzyme. mutant does not oxidize miltiradiene, reaction of EC 1.14.13.190
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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coexpression of mutant F112L or mutant V296L and cytochrome Cyp76AK6 in yeast leads to overall improvements of 24- and 14fold for pisiferic acid and salviol, respectively, compared to wild-type