ID   4.4.1.37
DE   pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
AN   P2CMN sulfurtransferase.
AN   P2TMN synthase.
AN   pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase.
CA   (1) [LarE protein]-L-cysteine + ATP + pyridinium-3,5-dicarboxylate
CA   mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+)
CA   + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide.
CA   (2) [LarE protein]-L-cysteine + ATP + pyridinium-3-carboxylate-5-
CA   thiocarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP +
CA   diphosphate + H(+) + pyridinium-3,5-bisthiocarboxylate mononucleotide.
CC   -!- This enzyme, found in Lactobacillus plantarum, is involved in the
CC       biosynthesis of a nickel-pincer cofactor.
CC   -!- The process starts when one enzyme molecule adenylates pyridinium-
CC       3,5-dicarboxylate mononucleotide (P2CMN) and covalently binds the
CC       adenylated product to an intrinsic cysteine residue.
CC   -!- Next, the enzyme cleaves the carbon-sulfur bond, liberating
CC       pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide (PCTMN) and
CC       leaving a 2-aminoprop-2-enoate (dehydroalanine) residue attached to
CC       the protein.
CC   -!- Since the cysteine residue is not regenerated in vivo, the enzyme is
CC       inactivated during the process.
CC   -!- A second enzyme molecule then repeats the process with PCTMN,
CC       adenylating it and covalently binding it to the same cysteine
CC       residue, followed by liberation of pyridinium-3,5-bisthiocarboxylate
CC       mononucleotide (P2TMN) and the inactivation of the second enzyme
CC       molecule.
DR   F9UST4, LARE_LACPL ;
//