ArticleScientific reports2020
Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling.Nature chemistry · 2026Article
- Structural and functional analysis of LarC, a CTP-dependent cyclometallase required for nickel-pincer nucleotide cofactor biosynthesis.Science advances · 2026Article
- Genomic context analysis enables the discovery of an unusual NAD-dependent racemase in phosphonate catabolism.The FEBS journal · 2025Article
- Structural Basis for the Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.ACS catalysis · 2025Article
- Article
- Unveiling 14 novel 2-hydroxy acid racemization and epimerization reactions in the lactate racemase superfamily.The Journal of biological chemistry · 2025Article
- A structural view of nickel-pincer nucleotide cofactor-related biochemistry.Critical reviews in biochemistry and molecular biology · 2024Review
- Group 13 ion coordination to pyridyl breaks the reduction potentialChemical science · 2023Article
- Structure of the LarB-Substrate Complex and Identification of a Reaction Intermediate during Nickel-Pincer Nucleotide Cofactor Biosynthesis.Biochemistry · 2023Article
- Structural and mutational characterization of a malate racemase from the LarA superfamily.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Irreversible inactivation of lactate racemase by sodium borohydride reveals reactivity of the nickel-pincer nucleotide cofactor.ACS catalysis · 2023Article
- Five decades of metalloenzymology.The Enzymes · 2023Review
- The nickel-pincer coenzyme of lactate racemase: A case study of uncovering cofactor structure and biosynthesis.Methods in enzymology · 2023Article
- Unveiling the mechanisms and biosynthesis of a novel nickel-pincer enzyme.Biochemical Society transactions · 2022Article
- Metal Homeostasis in Pathogenic Streptococci.Microorganisms · 2022Review
- Characterization of the nickel-inserting cyclometallase LarC from Moorella thermoacetica and identification of a cytidinylylated reaction intermediate.Metallomics : integrated biometal science · 2022Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Isomerization reactions are fundamental in biology. Lactate racemase, which isomerizes L- and D-lactate, is composed of the LarA protein and a nickel-containing cofactor, the nickel-pincer nucleotide (NPN). In this study, we show that LarA is part of a superfamily containing many different enzymes. We overexpressed and purified 13 lactate racemase homologs, incorporated the NPN cofactor, and assayed the isomerization of different substrates guided by gene context analysis. We discovered two malate racemases, one phenyllactate racemase, one α-hydroxyglutarate racemase, two D-gluconate 2-epimerases, and one short-chain aliphatic α-hydroxyacid racemase among the tested enzymes. We solved the structure of a malate racemase apoprotein and used it, along with the previously described structures of lactate racemase holoprotein and D-gluconate epimerase apoprotein, to identify key residues involved in substrate binding. This study demonstrates that the NPN cofactor is used by a diverse superfamily of α-hydroxyacid racemases and epimerases, widely expanding the scope of NPN-dependent enzymes.
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