ArticleNature communications2014
Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 122 citations in OpenAlex.
- Discovering nickel enzymes within the aldo-keto reductase superfamily.Nature chemistry · 2026Article
- 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
- Pheromone cCF10 Enhances Persister Formation inMicroorganisms · 2026Article
- D- and L-lactate consumers are taxonomically, biochemically, and energetically different.ISME communications · 2026Article
- High-ResolutionMolecules (Basel, Switzerland) · 2025Article
- 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
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- 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
- Association between organic nitrogen substrates and the optical purity of D-lactic acid during the fermentation by Sporolactobacillus terrae SBT-1.Scientific reports · 2024Article
- Structure-based insights into the mechanism of [4Fe-4S]-dependent sulfur insertase LarE.Protein science : a publication of the Protein Society · 2024Article
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- Article
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- 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
- Site Specialization of Human OralMicrobiology spectrum · 2023Article
- Irreversible inactivation of lactate racemase by sodium borohydride reveals reactivity of the nickel-pincer nucleotide cofactor.ACS catalysis · 2023Article
- Biofilm dysbiosis and caries activity: a surface or an individual issue?Journal of applied oral science : revista FOB · 2023Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Racemases catalyse the inversion of stereochemistry in biological molecules, giving the organism the ability to use both isomers. Among them, lactate racemase remains unexplored due to its intrinsic instability and lack of molecular characterization. Here we determine the genetic basis of lactate racemization in Lactobacillus plantarum. We show that, unexpectedly, the racemase is a nickel-dependent enzyme with a novel α/β fold. In addition, we decipher the process leading to an active enzyme, which involves the activation of the apo-enzyme by a single nickel-containing maturation protein that requires preactivation by two other accessory proteins. Genomic investigations reveal the wide distribution of the lactate racemase system among prokaryotes, showing the high significance of both lactate enantiomers in carbon metabolism. The even broader distribution of the nickel-based maturation system suggests a function beyond activation of the lactate racemase and possibly linked with other undiscovered nickel-dependent enzymes.
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