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Structure and Function of Benzylsuccinate Synthase and Related Fumarate-Adding Glycyl Radical Enzymes

Lookup NU author(s): Professor Bernard Golding

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Abstract

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


Publication metadata

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


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