Information on EC 1.14.13.149 - phenylacetyl-CoA 1,2-epoxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.149
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RECOMMENDED NAME
GeneOntology No.
phenylacetyl-CoA 1,2-epoxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylacetyl-CoA + NADPH + H+ + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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phenylacetate degradation I (aerobic)
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Phenylalanine metabolism
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phenylacetate degradation (aerobic)
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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.
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
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
epoxyphenylacetyl-CoA + O2 + NADPH + H+
?
show the reaction diagram
phenylacetyl-CoA + O2 + NADPH + H+
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme shows low affinity for iron, some rearrangement of the protein is induced by iron binding
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzoyl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.006
epoxyphenylacetyl-CoA
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at pH 8.0 and 30°C
0.023
NADPH
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at pH 8.0 and 30°C
0.003
O2
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at pH 8.0 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
dimer of heterodimers
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
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
Ni-NTA column chromatography and Superose 12 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Pseudomonas sp. strain Y2
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Show AA Sequence (171 entries)
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