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Literature summary for 5.3.3.18 extracted from

  • Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
    Bacterial phenylalanine and phenylacetate catabolic pathway revealed (2010), Proc. Natl. Acad. Sci. USA, 107, 14390-14395.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.3.18

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
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Pseudomonas sp. Y2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin Pseudomonas sp. 2-oxepin-2(3H)-ylideneacetyl-CoA
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 ?
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin Pseudomonas sp. Y2 2-oxepin-2(3H)-ylideneacetyl-CoA
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 ?

Synonyms

Synonyms Comment Organism
paaG
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 Pseudomonas sp.