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Information on EC 3.3.2.12 - oxepin-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P77455
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3.3.2.12 oxepin-CoA hydrolaseIUBMB Comments
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 1.17.1.7, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase.Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway [1,3,4]. The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate .
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
EC 3.7.1.16, ECH-Aa, MaoC, oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+), paaZ, PaaZ-ECH, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+)
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+)
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bifunctional fusion proteom
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+)
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bifunctional protein
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
2-oxepin-2(3H)-ylideneacetyl-CoA hydrolyase
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 1.17.1.7, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase.Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway [1,3,4]. The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate [2].
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
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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-
-
?
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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addition of purified PaaZ enzyme to enzymatically produced epoxide and oxepin in the presence of PaaG protein leads to a complete NADP+-dependent conversion of epoxide and oxepin into 3-oxo-5,6-dehydrosuberyl-CoA. PaaZ functions as an oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase catalyzing the two-step conversion of the oxepin-CoA via the open-chain aldehyde intermediate to 3-oxo-5,6-dehydrosuberyl-CoA
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-
?
crotonyl-CoA + H2O
(R)-3-hydroxybutyryl-CoA
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the enzyme shows 1% activity with crotonyl-CoA compared to oxepin-CoA
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-
?
oxepin-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
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100% activity
main product
-
?
additional information
?
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-
bifunctional protein, catalyzing the reactions of 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase, EC 3.3.2.12, and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase, EC 1.17.1.7
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-
?
additional information
?
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bifunctional protein, catalyzing the reactions of 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase, EC 3.3.2.12, and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase, EC 1.17.1.7
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-
?
additional information
?
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the bifunctional protein also use 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and NADP+ as substrate yielding 3-oxo-5,6-dehydrosuberyl-CoA as main product
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-
?
additional information
?
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the bifunctional protein also use 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and NADP+ as substrate yielding 3-oxo-5,6-dehydrosuberyl-CoA as main product. The PaaZ-ECH domain acts as (R)-specific hydratase and shows no activity with (S)-3-hydroxybutyryl-CoA
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-
?
additional information
?
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enzyme additionally shows enoyl-CoA hydratase activity involved in supplying (R)-3-hydroxyacyl-CoA from the beta-oxidation pathway to polyhydroxyalkanoate biosynthetic pathway in the fadB mutant Escherichia coli strain
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
-
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional protein, catalyzing the reactions of 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase, EC 3.3.2.12, and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase, EC 1.17.1.7
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
the paaZ gene product is responsible of the third enzymatic step in the aerobic catabolism of phenylacetate in Escherichia coli
physiological function
physiological function
mutants with a deletion of the paaF, paaG, paaH, paaJ or paaZ gene are unable to grow with phenylacetate as carbon source. The paaG and paaZ mutants convert phenylacetate into ortho-hydroxyphenylacetate. Results suggest a catabolic pathway via CoA thioesters. Phenylacetyl-CoA is attacked by a ring-oxygenase/reductase, PaaABCDE proteins, generating a hydroxylated and reduced derivative of phenylacetyl-CoA, which is not re-oxidized to a dihydroxylated aromatic intermediate but is further metabolized in a complex reaction sequence comprising enoyl-CoA isomerization/hydration, nonoxygenolytic ring opening, and dehydrogenation catalyzed by the PaaG and PaaZ proteins. The subsequent beta-oxidation-type degradation of the resulting CoA dicarboxylate via beta-ketoadipyl-CoA to succinyl-CoA and acetyl-CoA appears to be catalyzed by the PaaJ, PaaF and PaaH proteins
physiological function
the paaZ gene product is responsible of the third enzymatic step in the aerobic catabolism of phenylacetic acid
malfunction
disruption of the paaZ gene causes a blockade of the phenylacetate catabolic pathway
malfunction
Eschericha coli K12 mutants with a deletion of the paaZ gene are unable to grow with phenylacetate as carbon source. The paaZ mutant converts phenylacetate into ortho-hydroxyphenylacetate
physiological function
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a fadB maoC double-mutant strain, lacking fatty acid oxidation complex protein FadB and the enzyme, accumulates 43% less amount of medium-chain-length polyhydroxyalkanoates from fatty acid compared with the fadB mutant
physiological function
-
enzyme is part of the catabolic pathway of phenylacetate. Intermediates are processed as CoA thioesters, and the aromatic ring of phenylacetyl-CoA becomes activated to a ring 1,2-epoxide by a distinct multicomponent oxygenase. The reactive nonaromatic epoxide is isomerized to a seven-member O-heterocyclic enol ether, an oxepin. This isomerization is followed by hydrolytic ring cleavage and beta-oxidation steps, leading to acetyl-CoA and succinyl-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-affinity column chromatography or amylose resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, S.J.; Lee, S.Y.
Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli
J. Bacteriol.
185
5391-5397
2003
Escherichia coli
Ismail, W.; El-Said Mohamed, M.; Wanner, B.; Datsenko, K.; Eisenreich, W.; Rohdich, F.; Bacher, A.; Fuchs, G.
Functional genomics by NMR spectroscopy: Phenylacetate catabolism in Escherichia coli
Eur. J. Biochem.
270
3047-3054
2003
Escherichia coli, Escherichia coli (P77455)
Ferrandez, A.; Minambres, B.; Garcia, B.; Olivera, E.; Luengo, J.; Garcia, J.; Diaz, E.
Catabolism of phenylacetic acid in Escherichia coli: Characterization of a new aerobic hybrid pathway
J. Biol. Chem.
273
25974-25986
1998
Escherichia coli, Escherichia coli (P77455), Escherichia coli W14
Teufel, R.; Gantert, C.; Voss, M.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
Studies on the mechanism of ring hydrolysis in phenylacetate degradation: A metabolic branching point
J. Biol. Chem.
286
11021-11034
2011
Escherichia coli
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Release 2023.1 (January 2023)
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