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Information on EC 5.3.3.18 - 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase and Organism(s) Escherichia coli and UniProt Accession P77467

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IUBMB Comments
The enzyme catalyses the reversible isomerization of 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA to the unusual unsaturated, oxygen-containing, seven-member heterocyclic enol ether 2-oxepin-2(3H)-ylideneacetyl-CoA, as part of an aerobic phenylacetate degradation pathway.
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Escherichia coli
UNIPROT: P77467
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
paaG, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase
The enzyme catalyses the reversible isomerization of 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA to the unusual unsaturated, oxygen-containing, seven-member heterocyclic enol ether 2-oxepin-2(3H)-ylideneacetyl-CoA, as part of an aerobic phenylacetate degradation pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mutants with a deletion of paaG gene are unable to grow on phenylacetate as carbon source. Incubation of a paaG mutant with [U-13C8]phenylacetate yields ring-1,2-dihydroxy-1,2-dihydrophenylacetyl lactone. The paaG mutant also converts phenylacetate into ortho-hydroxyphenylacetate, a dead end product of phenylacetate catabolism. The catabolic pathway of phenylacetate involves CoA thioesters. Phenylacetyl-CoA is attacked by a ring-oxygenase/reductase, PaaABCDE proteins, generating a hydroxylated and reduced derivative of phenylacetyl-CoA. The intermediate CoA ester 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P77467)
Manually annotated by BRENDA team