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ENZYME entry: EC

Accepted Name
Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
Alternative Name(s)
P2CMN sulfurtransferase.
P2TMN synthase.
Pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase.
Reaction catalysed
  • [LarE]-L-cysteine + pyridinium-3,5-dicarboxylate mononucleotide + ATP <=> [LarE]-dehydroalanine + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate
  • [LarE]-L-cysteine + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP <=> [LarE]-dehydroalanine + pyridinium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate
  • This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor.
  • The process starts when one enzyme molecule adenylates pyridinium- 3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the adenylated product to an intrinsic cysteine residue.
  • Next, the enzyme cleaves the carbon-sulfur bond, liberating pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to the protein.
  • Since the cysteine residue is not regenerated in vivo, the enzyme is inactivated during the process.
  • A second enzyme molecule then repeats the process with PCTMN, adenylating it and covalently binding it to the same cysteine residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule.
PRIAM enzyme-specific profiles4.4.1.37
KEGG Ligand Database for Enzyme Nomenclature4.4.1.37
IUBMB Enzyme Nomenclature4.4.1.37
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