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

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.13.108
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RECOMMENDED NAME
GeneOntology No.
abieta-7,13-diene hydroxylase
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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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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abietic acid biosynthesis
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Biosynthesis of secondary metabolites
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Diterpenoid biosynthesis
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Metabolic pathways
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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].
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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
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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
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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
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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
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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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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042
abietadiene
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pH 7.5, 32°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0093
Ancymidol
Abies grandis
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pH 7.5, 32°C
0.0005
clotrimazole
Abies grandis
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pH 7.5, 32°C
0.0009
cytochrome c
Abies grandis
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pH 7.5, 32°C
0.005
Metyrapone
Abies grandis
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pH 7.5, 32°C
0.307
miconazole
Abies grandis
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pH 7.5, 32°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.6
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-
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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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.108)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)