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Enzyme Nomenclature
Information on EC 1.14.13.149 - phenylacetyl-CoA 1,2-epoxidase
Word Map on EC 1.14.13.149
- 1.14.13.149
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phenylacetic
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monooxygenase
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multicomponent
- oxygenase
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phenylacetyl-coenzyme
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pa-coa
- epoxide
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subcomplexes
- phenylalanine
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di-iron
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ligand-free
- burkholderia
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microbes
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.149
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RECOMMENDED NAME
GeneOntology No.
phenylacetyl-CoA 1,2-epoxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylacetyl-CoA + NADPH + H+ + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing)
Part of the aerobic pathway of phenylacetate catabolism in Escherichia coli and Pseudomonas putida.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
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bifunctional PaaABCE acts as a phenylacetyl-CoA ring-1,2-epoxidase/ring-1,2-epoxyphenylacetyl-CoA deoxygenase
metabolism
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bifunctional PaaABCE acts as a phenylacetyl-CoA ring-1,2-epoxidase/ring-1,2-epoxyphenylacetyl-CoA deoxygenase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
epoxyphenylacetyl-CoA + O2 + NADPH + H+
?
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the di-iron center of PaaABCE also deoxygenates epoxyphenylacetyl-CoA, which occurs when phenylacetyl-CoA is largely used up
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?
epoxyphenylacetyl-CoA + O2 + NADPH + H+
?
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the di-iron center of PaaABCE also deoxygenates epoxyphenylacetyl-CoA, which occurs when phenylacetyl-CoA is largely used up
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?
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
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ir
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
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true substrate
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?
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
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?
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
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?
additional information
?
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he non-physiological substrate benzoyl-CoA is not transformed to detectable products
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additional information
?
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he non-physiological substrate benzoyl-CoA is not transformed to detectable products
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
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the enzyme shows low affinity for iron, some rearrangement of the protein is induced by iron binding
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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maltose-binding protein-tagged PaaD added separately does not affect the specific activity of PaaABCE significantly
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the absence of a bound ligand (with 100 mM N-(2-acetamido)-iminodiacetic acid pH 5.5) as well as in complexes with CoA, 3-hydroxybutyryl-CoA, benzoyl-CoA and phenylacetyl-CoA, using either 0.1 M PIPES pH 6.5, 15% (w/v) PEG 550 monomethyl ether or 0.1 M PIPES pH 6.5, 5% (v/v) 2-propanol, 5% (w/v) PEG 550 monomethyl ether
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hanging drop vapor diffusion method, PaaAC with acetyl-CoA is crystallized in 0.1 M sodium citrate buffer, pH 5.5, and 15% (w/v) PEG 6000 (Fluka). Crystals of ligand-free PaaAC are obtained in 100 mM N-(2-acetamido)-iminodiacetic acid, pH 5.5
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the ability of PaaABC(D)E to oxygenate its substrate is largely lost within 5 min in an enzymatic assay (50 mMTris-HCl (pH 8.0) at 30°C)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.149)
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