| EC |
4.99.1.12 |
| Accepted name: |
pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase |
| Reaction: |
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide = pyridinium-3,5-bisthiocarboxylate mononucleotide + Ni2+ |
| Other name(s): |
LarC; P2TMN nickel chelatase |
| Systematic name: |
Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide nickel-lyase (pyridinium-3,5-bisthiocarboxylate-mononucleotide-forming) |
| Comments: |
This enzyme, found in Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor. It catalyses the insertion of Ni2+ into the cofactor forming a covalent bond between a carbon atom and the nickel atom. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Desguin, B., Goffin, P., Viaene, E., Kleerebezem, M., Martin-Diaconescu, V., Maroney, M.J., Declercq, J.P., Soumillion, P. and Hols, P. Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system. Nat. Commun. 5:3615 (2014). [DOI] [PMID: 24710389] |
| 2. |
Desguin, B., Soumillion, P., Hols, P. and Hausinger, R.P. Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion. Proc. Natl. Acad. Sci. USA 113 (2016) 5598–5603. [DOI] [PMID: 27114550] |
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| [EC 4.99.1.12 created 2017] |
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