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Phenylacetate decarboxylase
From Wikipedia, the free encyclopedia
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Phenylacetate decarboxylase is a carboxy-lyase enzyme. The enzyme was isolated from anoxic toluene-producing microbial communities. It is a glycyl radical enzyme.[1][2] It requires activation through a dedicated cognate activating enzyme (encoded by PhdA). The cognate activase catalyses the reductive lysing of S-Adenosyl methionine which yields a 5'-deoxyadenosyl radical that allows the production of the glycyl radical.[3] The enzyme catalyzes the following reaction:
- Phenylacetate + H+ = Toluene + CO2
The enzyme is involved in various biosynthetic and bio-catabolic pathways, including the toluene production pathway, phenylacetate degradation pathway and biosynthetic pathway of select other aromatic compounds in toluene (and other aromatic carbon) producing bacterial species.[4]
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