ENZYME entry: EC 18.104.22.168
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|Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase.
|Pyridinium-3,5-biscarboxylic acid mononucleotide sulfurtransferase.|
- [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
- 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
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 4.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-