Information on EC 1.14.13.108 - abieta-7,13-diene hydroxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.108
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RECOMMENDED NAME
GeneOntology No.
abieta-7,13-diene hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
abieta-7,13-diene + NADPH + H+ + O2 = abieta-7,13-dien-18-ol + NADP+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abietic acid biosynthesis
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Diterpenoid biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
abieta-7,13-diene,NADPH:oxygen oxidoreductase (18-hydroxylating)
A heme-thiolate protein (P-450). This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). The enzyme is localized in the microsomal fraction and requires both oxygen and NADPH. Inhibition by carbon monoxide and several substituted N-heterocyclic inhibitors suggests that the enzyme is a cytochrome P-450-dependent monooxygenase [1]. Activity is induced by wounding of the plant tissue [2].
CAS REGISTRY NUMBER
COMMENTARY hide
160477-92-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Lindl.
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Manually annotated by BRENDA team
Douglas var. latifolia Engelman
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
abietadiene + NADPH + H+ + O2
abietadienol + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
abietadiene + NADPH + H+ + O2
abietadienol + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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cytochrome P-450-dependent monooxygenase
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FAD
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omission of flavins results in measurable reduction in both hydroxylation activities
FMN
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omission of flavins results in measurable reduction in both hydroxylation activities
NADH
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hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant
NADPH
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hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ancymidol
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clotrimazole
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CO
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blue light reversible inhibition
cytochrome c
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Metyrapone
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miconazole
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042
abietadiene
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pH 7.5, 32C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0093
Ancymidol
Abies grandis
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pH 7.5, 32C
0.0005
clotrimazole
Abies grandis
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pH 7.5, 32C
0.0009
cytochrome c
Abies grandis
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pH 7.5, 32C
0.005
Metyrapone
Abies grandis
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pH 7.5, 32C
0.307
miconazole
Abies grandis
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pH 7.5, 32C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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60-70% of maximal activity at pH 7.0 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE