The Enzyme Database

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Accepted name: phenylacetate decarboxylase
Reaction: phenylacetate = toluene + CO2
Other name(s): phdB (gene name)
Systematic name: phenylacetate carboxy-lyase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Zargar, K., Saville, R., Phelan, R.M., Tringe, S.G., Petzold, C.J., Keasling, J.D. and Beller, H.R. In vitro characterization of phenylacetate decarboxylase, a novel enzyme catalyzing toluene biosynthesis in an anaerobic microbial community. Sci. Rep. 6:31362 (2016). [PMID: 27506494]
2.  Beller, H.R., Rodrigues, A.V., Zargar, K., Wu, Y.W., Saini, A.K., Saville, R.M., Pereira, J.H., Adams, P.D., Tringe, S.G., Petzold, C.J. and Keasling, J.D. Discovery of enzymes for toluene synthesis from anoxic microbial communities. Nat. Chem. Biol. 14 (2018) 451–457. [PMID: 29556105]
3.  Rodrigues, A.V., Tantillo, D.J., Mukhopadhyay, A., Keasling, J.D. and Beller, H. Insights into the mechanism of phenylacetate decarboxylase (PhdB), a toluene-producing glycyl radical enzyme. ChemBioChem (2019) . [PMID: 31512343]
[EC created 2019]

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