Staphylopine dehydrogenase
| Staphylopine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.52 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Staphylopine synthase (EC 1.5.1.52) is an enzyme that catalyzes NADPH-dependent reductive condensation of pyruvate to the intermediate (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate, which is the last step in the biosynthesis of the metallophore staphylopine.[1] The chemical reaction is:
- H2O + NADP+ + staphylopine = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H+ + NADPH + pyruvate[2]
Alternative name(s): staphylopine dehydrogenase.
References
- ^ Ghssein, G.; Brutesco, C.; Ouerdane, L.; Fojcik, C.; Izaute, A.; Wang, S.; Hajjar, C.; Lobinski, R.; Lemaire, D.; Richaud, P.; Voulhoux, R. (2016-05-26). "Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus" (PDF). Science. 352 (6289): 1105–1109. Bibcode:2016Sci...352.1105G. doi:10.1126/science.aaf1018. ISSN 0036-8075. PMID 27230378. S2CID 5525387.
- ^ "cntM – Staphylopine synthase – Staphylococcus aureus (strain Mu50 / ATCC 700699) – cntM gene & protein". www.uniprot.org. Retrieved 2019-12-03.