EC - Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase

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IntEnz Enzyme Nomenclature


Accepted name:
pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase
Other names:
P2TMN nickel chelatase
Systematic name:
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide nickel-lyase (pyridinium-3,5-bisthiocarboxylate-mononucleotide forming)



This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It catalyses the insertion of Ni2+ into the cofactor forming a covalent bond between a carbon atom and the nickel atom.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (21) [show] [UniProt]


  1. Desguin, B., Goffin, P., Viaene, E., Kleerebezem, M., Martin-Diaconescu, V., Maroney, M. J., Declercq, J. P., Soumillion, P., Hols, P.
    Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system.
    Nat Commun 5 : 3615 (2014). [PMID: 24710389]
  2. Desguin, B., Soumillion, P., Hols, P., Hausinger, R. P.
    Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion.
    Proc. Natl. Acad. Sci. U.S.A. 113 : 5598-5603 (2016). [PMID: 27114550]

[EC created 2017]