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 protein]-L-cysteine + ATP + pyridinium-3,5-dicarboxylate mononucleotide <=> [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide
- [LarE protein]-L-cysteine + ATP + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide <=> [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3,5-bisthiocarboxylate mononucleotide
|
Comment(s) |
- 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.
|
Cross-references |
BRENDA | 4.4.1.37 |
EC2PDB | 4.4.1.37 |
ExplorEnz | 4.4.1.37 |
PRIAM enzyme-specific profiles | 4.4.1.37 |
KEGG Ligand Database for Enzyme Nomenclature | 4.4.1.37 |
IUBMB Enzyme Nomenclature | 4.4.1.37 |
IntEnz | 4.4.1.37 |
MEDLINE | Find literature relating to 4.4.1.37 |
MetaCyc | 4.4.1.37 |
Rhea expert-curated reactions | 4.4.1.37 |
UniProtKB/Swiss-Prot |
|
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