Nickel-pincer nucleotide cofactor.

Robert P Hausinger, Benoît Desguin, Matthias Fellner, Joel A Rankin, Jian Hu

Journal: Current opinion in chemical biology 2019;47():18-23

PMID: 30015232

Full Text on Elsevier Science View on PubMed

Abstract

A novel organometallic cofactor, nickel pyridinium-3,5-dithiocarboxylic acid mononucleotide, was recently discovered in lactate racemase (LarA) of Lactobacillus plantarum. This review summarizes the substantial progress made in uncovering the function of this cofactor as a transient hydride acceptor in the LarA mechanism. The latest developments related to cofactor biosynthesis reveal insights into a pathway in which LarB serves as a nicotinic acid adenine dinucleotide hydrolase/carboxylase, LarE acts as a sacrificial sulfur transferase, and LarC functions as a nickel insertase, forming the nickel-pincer nucleotide cofactor that becomes covalently tethered to LarA in some bacteria. Bioinformatic studies reveal a widespread occurrence of larA, larB, larC, and larE orthologs in microorganisms, and additional roles for the cofactor are considered.

Address: Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. Electronic address: [email protected].; Institute of Life Sciences, Université catholique de Louvain, B-1348 Louvain-La-Neuve, Belgium.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.; Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA; Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.

DOI: 10.1016/j.cbpa.2018.06.019

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MeSH Terms: Coenzymes, Lactobacillus plantarum, Models, Molecular, Nickel, Nucleotides, Organometallic Compounds, Racemases and Epimerases