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The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 126.96.36.199, 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 .
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
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
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
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
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
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