ArticleProceedings of the National Academy of Sciences of the United States of America2016
Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 56 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
- Functional divergence and conservation in the QueC protein family (PF06508): from tRNA modification to anti-phage defense.The Biochemical journal · 2026Article
- Functional Divergence and Conservation in the QueC Protein Family (PF06508): From tRNA Modification to Anti-Phage Defense.bioRxiv : the preprint server for biology · 2026Article
- Assessment of the impact of manual curation in BioCyc.Frontiers in bioinformatics · 2026Article
- 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
- Culturable Bacterial Endophytes of Wild White Poplar (Biology · 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
- 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
- Characterization of the nickel-inserting cyclometallase LarC from Moorella thermoacetica and identification of a cytidinylylated reaction intermediate.Metallomics : integrated biometal science · 2022Article
- The LarB carboxylase/hydrolase forms a transient cysteinyl-pyridine intermediate during nickel-pincer nucleotide cofactor biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Uncovering a superfamily of nickel-dependent hydroxyacid racemases and epimerases.Scientific reports · 2020Article
- An Unusual Route forJournal of bacteriology · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lactate racemase enzyme (LarA) of Lactobacillus plantarum harbors a (SCS)Ni(II) pincer complex derived from nicotinic acid. Synthesis of the enzyme-bound cofactor requires LarB, LarC, and LarE, which are widely distributed in microorganisms. The functions of the accessory proteins are unknown, but the LarB C terminus resembles aminoimidazole ribonucleotide carboxylase/mutase, LarC binds Ni and could act in Ni delivery or storage, and LarE is a putative ATP-using enzyme of the pyrophosphatase-loop superfamily. Here, we show that LarB carboxylates the pyridinium ring of nicotinic acid adenine dinucleotide (NaAD) and cleaves the phosphoanhydride bond to release AMP. The resulting biscarboxylic acid intermediate is transformed into a bisthiocarboxylic acid species by two single-turnover reactions in which sacrificial desulfurization of LarE converts its conserved Cys176 into dehydroalanine. Our results identify a previously unidentified metabolic pathway from NaAD using unprecedented carboxylase and sulfur transferase reactions to form the organic component of the (SCS)Ni(II) pincer cofactor of LarA. In species where larA is absent, this pathway could be used to generate a pincer complex in other enzymes.
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