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Lookup NU author(s): Emeritus Professor Bernard Golding
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The pathway of anaerobic toluene degradation is initiated by a remarkable radical-type enantiospecific addition of the chemically inert methyl group to the double bond of a fumarate cosubstrate to yield (R)-benzylsuccinate as the first intermediate, as catalyzed by the glycyl radical enzyme benzylsuccinate synthase. In recent years, it has become clear that benzylsuccinate synthase is the prototype enzyme of a much larger family of fumarate-adding enzymes, which play important roles in the anaerobic metabolism of further aromatic and even aliphatic hydrocarbons. We present an overview on the biochemical properties of benzylsuccinate synthase, as well as its recently solved structure, and present the results of an initial structure-based modeling study on the reaction mechanism. Moreover, we compare the structure of benzylsuccinate synthase with those predicted for different clades of fumarate-adding enzymes, in particular the paralogous enzymes converting p-cresol, 2-methylnaphthalene or n-alkanes. (C) 2016 S. Karger AG, Basel
Author(s): Heider J, Szaleniec M, Martins BM, Seyhan D, Buckel W, Golding BT
Publication type: Review
Publication status: Published
Journal: Journal of Molecular Microbiology and Biotechnology
Year: 2016
Volume: 26
Issue: 1-3
Pages: 29-44
Print publication date: 01/03/2016
Online publication date: 01/03/2016
Acceptance date: 01/01/1900
ISSN (print): 1464-1801
ISSN (electronic): 1660-2412
Publisher: KARGER
URL: http://dx.doi.org/10.1159/000441656
DOI: 10.1159/000441656
