This bacterial enzyme, isolated from anoxic, toluene-producing microbial communities, is a glycyl radical enzyme. It needs to be activated by a dedicated activating enzyme (PhdA). The activase catalyses the reductive cleavage of AdoMet, producing a 5'-deoxyadenosyl radical that leads to the production of the glycyl radical in PhdB.
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The expected taxonomic range for this enzyme is: uncultured bacterium
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SYSTEMATIC NAME
IUBMB Comments
phenylacetate carboxy-lyase
This bacterial enzyme, isolated from anoxic, toluene-producing microbial communities, is a glycyl radical enzyme. It needs to be activated by a dedicated activating enzyme (PhdA). The activase catalyses the reductive cleavage of AdoMet, producing a 5'-deoxyadenosyl radical that leads to the production of the glycyl radical in PhdB.
mechanism follows attack of the phenylacetate methylene carbon rather than attack of the carboxylate group via a Kolbe-type decarboxylation (single-electron oxidation) or hydrogen-atom abstraction from the protonated carboxyl group
toluene-producing enzyme PhdB is a glycyl radical enzyme of bacterial origin that catalyzes phenylacetate decarboxylation. Its cognate activating enzyme is PhdA, a radical S-adenosylmethionine enzyme, discovered in two distinct anoxic microbial communities that produce toluene
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of the substrate-bound active sites of PhdB. Important conserved residues, are the sites of the thiyl radical, Cys482 and glycyl radical ,Gly815. PhdB has a hydrophobic pocket including Trp495, Tyr691, and Val693 accommodating the unsubstituted ring of phenylacetate
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History
Enzyme Nomenclature
4.1.1.119 phenylacetate decarboxylase
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