Literature summary for 3.3.2.12 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.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni2+-affinity column chromatography or amylose resin column chromatography	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.02	-	pH not specified in the publication, temperature not specified in the publication	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O	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	Escherichia coli	3-oxo-5,6-dehydrosuberyl-CoA semialdehyde	-	?
additional information	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	Escherichia coli	?	-	?
oxepin-CoA + H2O	-	Escherichia coli	3-oxo-5,6-dehydrosuberyl-CoA semialdehyde	-	?

Synonyms

Synonyms	Comment	Organism
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+)	bifunctional protein	Escherichia coli
paaZ	-	Escherichia coli

General Information

General Information	Comment	Organism
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	Escherichia coli

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Release 2023.1 (January 2023)