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Gyroid Nickel Nanostructures from Diblock Copolymer Supramolecules
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Nickel-pincer nucleotide cofactor.

Robert P Hausinger1, Benoît Desguin2, Matthias Fellner3

  • 1Department 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.

Current Opinion in Chemical Biology
|July 18, 2018
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Summary
This summary is machine-generated.

A new nickel cofactor in lactate racemase (LarA) acts as a hydride acceptor. Its biosynthesis involves LarB, LarE, and LarC, with widespread microbial distribution.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbiology

Background:

  • A novel organometallic cofactor, nickel pyridinium-3,5-dithiocarboxylic acid mononucleotide, has been identified in lactate racemase (LarA).
  • This cofactor plays a crucial role in the enzymatic mechanism of LarA.

Purpose of the Study:

  • To review the progress in understanding the function of this nickel cofactor.
  • To elucidate the biosynthesis pathway and explore potential additional roles of the cofactor.

Main Methods:

  • Literature review of recent findings on the nickel cofactor and LarA.
  • Analysis of cofactor biosynthesis pathways involving LarB, LarE, and LarC.
  • Bioinformatic analysis of larA, larB, larC, and larE orthologs distribution.

Main Results:

  • The nickel cofactor functions as a transient hydride acceptor in the LarA mechanism.
  • Cofactor biosynthesis involves LarB (hydrolase/carboxylase), LarE (sulfur transferase), and LarC (nickel insertase).
  • The nickel-pincer nucleotide cofactor is covalently attached to LarA in some bacteria.

Conclusions:

  • The review summarizes the current understanding of the nickel cofactor's function and biosynthesis.
  • Bioinformatic data indicate a broad distribution of related genes in microorganisms.
  • Further investigation into additional roles of this cofactor is warranted.