New tricks for the glycyl radical enzyme family
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Author(s) • • •
Funk, Michael A.
Backman, Lindsey R.
Dawson, Christopher Daniel
Drennan, Catherine L.
Date Issued
September 2017
Journal
Critical Reviews in Biochemistry and Molecular Biology
Publisher
Informa UK Limited
Citation
Backman, Lindsey R. F. et al. “New Tricks for the Glycyl Radical Enzyme Family.” Critical Reviews in Biochemistry and Molecular Biology 52, 6 (September 2017): 674–695 © 2017 Informa UK Limited, trading as Taylor & Francis Group
Version
Author's final manuscript
Abstract
Glycyl radical enzymes (GREs) are important biological catalysts in both strict and facultative anaerobes, playing key roles both in the human microbiota and in the environment. GREs contain a backbone glycyl radical that is post-translationally installed, enabling radical-based mechanisms. GREs function in several metabolic pathways including mixed acid fermentation, ribonucleotide reduction and the anaerobic breakdown of the nutrient choline and the pollutant toluene. By generating a substrate-based radical species within the active site, GREs enable C–C, C–O and C–N bond breaking and formation steps that are otherwise challenging for nonradical enzymes. Identification of previously unknown family members from genomic data and the determination of structures of well-characterized GREs have expanded the scope of GRE-catalyzed reactions as well as defined key features that enable radical catalysis. Here, we review the structures and mechanisms of characterized GREs, classifying members into five categories. We consider the open questions about each of the five GRE classes and evaluate the tools available to interrogate uncharacterized GREs. Keywords: Glycyl radical enzymes; radical chemistry; anaerobic metabolism; pyruvate formate-lyase; class III ribonucleotide reductase; choline trimethylamine-lyase; benzylsuccinate synthase; radical decarboxylases
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1080/10409238.2017.1373741