Lactate Racemase Nickel-Pincer Cofactor Operates by a Proton-Coupled Hydride Transfer Mechanism
Author:
Affiliation:
1. Department of Chemistry, University of Nevada, Reno, Nevada 89557, United States
2. Institute of Life Sciences, Université catholique de Louvain, B-1348 Louvain-La-Neuve, Belgium
Funder
Division of Chemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00100
Reference35 articles.
1. Enzymic racemization of optically active lactic acid
2. A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase
3. Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion
4. Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system
5. Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE
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