Information on EC 5.3.3.18 - 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.3.18
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RECOMMENDED NAME
GeneOntology No.
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-oxepin-2(3H)-ylideneacetyl-CoA
show the reaction diagram
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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
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
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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
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
2-oxepin-2(3H)-ylideneacetyl-CoA
show the reaction diagram
additional information
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enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism
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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
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
2-oxepin-2(3H)-ylideneacetyl-CoA
show the reaction diagram
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r
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28779
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3 * 28779, MALDI-TOF mass spectrometry
30000
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3 * 30000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
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3 * 28779, MALDI-TOF mass spectrometry; 3 * 30000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M sodium citrate, pH 5.5, 0.2 M sodium acetate, and 5% (w/w) PEG 4000
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to 1.85 A resolution. Enzyme consists of three identical subunits related by local three-fold symmetry. The monomer is comprised of a spiral and a helical domain with a fold characteristic of the crotonase superfamily. A putative active site residue, Asp136, is situated in an active site cavity and surrounded by several hydrophobic and hydrophilic residues. The active site cavity is sufficiently large to accommodate a ring substrate. Two conformations are observed for helix H2 located adjacent to the active site. Helix H2 is kinked at Asn81 in two subunits, whereas it is kinked at Leu77 in the other subunit, and the side chain of Tyr80 is closer to Asp136. This indicates that catalytic reaction of PaaG may proceed with large conformational changes at the active site
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA beads chromatography and Superdex 200 gel filtration
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Show AA Sequence (322 entries)
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