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| Parent Class: | EC-Numbers → 4 -- Lyases → 4.4 -- Carbon-sulfur lyases → 4.4.1 -- Carbon-sulfur lyases |
Synonyms: LarE, P2CMN sulfurtransferase, pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase, P2TMN synthase
Systematic Name: [LarE]-S-[1-(5-O-phosphono-β-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium-3-carbonyl]-L-cysteine pyridin-1-ium-3,5-dicarbothioate-mononucleotide-lyase (ATP-consuming)
Unification Links: BRENDA:4.4.1.37, ENZYME:4.4.1.37, IUBMB-ExplorEnz:4.4.1.37
Reaction:
a [LarE]-L-cysteine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + ATP → a [LarE]-dehydroalanine + pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide + AMP + diphosphate + H+,
a [LarE]-L-cysteine + pyridin-1-ium-3,5-dicarboxylate mononucleotide + ATP → a [LarE]-dehydroalanine + pyridin-1-ium-3-carboxylate-5-thiocarboxylate mononucleotide + AMP + diphosphate + H+
Enzymes and Genes:
intrinsic cysteine-dependent pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase:
larE (
Lactiplantibacillus plantarum
)
Summary:
This enzyme, found in
Lactobacillus plantarum, catalyses two complex reactions during the biosynthesis of a nickel-pincer cofactor. The process starts when one enzyme molecule adenylates
pyridin-1-ium-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
pyridin-1-ium-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
pyridin-1-ium-3,5-bisthiocarboxylate mononucleotide (P2TMN) and the inactivation of the second enzyme molecule. cf
EC 4.4.1.45, extrinsic cysteine-dependent pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
Citations: [Desguin16]
References
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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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