EC Number   |
General Information |
Reference |
|---|
   3.3.2.12 | malfunction |
disruption of the paaZ gene causes a blockade of the phenylacetate catabolic pathway |
-, 715437 |
| 3.3.2.12 | malfunction |
Eschericha coli K12 mutants with a deletion of the paaZ gene are unable to grow with phenylacetate as carbon source. The paaZ mutant converts phenylacetate into ortho-hydroxyphenylacetate |
714891 |
| 3.3.2.12 | metabolism |
the paaZ gene product is responsible of the third enzymatic step in the aerobic catabolism of phenylacetate in Escherichia coli |
-, 715437 |
| 3.3.2.12 | physiological function |
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 |
651723 |
| 3.3.2.12 | 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 |
716755 |
| 3.3.2.12 | physiological function |
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 |
714891 |
| 3.3.2.12 | physiological function |
the paaZ gene product is responsible of the third enzymatic step in the aerobic catabolism of phenylacetic acid |
715437 |
