Information on EC 1.14.13.58 - benzoyl-CoA 3-monooxygenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.13.58
-
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RECOMMENDED NAME
GeneOntology No.
benzoyl-CoA 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + NADPH + H+ + O2 = 3-hydroxybenzoyl-CoA + NADP+ + H2O
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-phenylpropanoate degradation
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-
3-phenylpropionate degradation
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-
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SYSTEMATIC NAME
IUBMB Comments
benzoyl-CoA,NADPH:oxygen oxidoreductase (3-hydroxylating)
The enzyme from the denitrifying bacterium Pseudomonas KB740 catalyses a flavin-requiring reaction (FAD or FMN). Benzoate is not a substrate.
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CAS REGISTRY NUMBER
COMMENTARY hide
151616-61-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KB740
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-
Manually annotated by BRENDA team
strain KB740
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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
benzoyl-CoA + NADPH + O2
3-hydroxybenzoyl-CoA + NADP+ + H2O
show the reaction diagram
Benzoyl-CoA + NADPH + O2
?
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
Benzoyl-CoA + NADPH + O2
?
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
reaction is strictly dependent on the presence of a flavin nucleotide, FMN or FAD as cofactor
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
benzoyl-CoA
-
-
0.125
NADPH
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.025
-
-
1.812
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
50% of maximal activity at pH 6.5 and at pH 8.5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63000
-
1 * 63000, SDS-PAGE
65000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50% loss of activity after 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.58)
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)