UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase
| UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.7 | ||||||||
| CAS number | 9023-51-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase (EC 6.3.2.7) is an enzyme that catalyzes the chemical reaction
- ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate, and L-lysine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine gamma-ligase (ADP-forming). Other names in common use include MurE synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamyllysine, synthetase, and UPD-MurNAc-L-Ala-D-Glu:L-Lys ligase. This enzyme participates in peptidoglycan biosynthesis.
References
- Ito E, Strominger JL (1962). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides I. Enzymatic addition of L-alanine, D-glutamic acid, and L-lysine". J. Biol. Chem. 237: 2689&ndash, 2695.
- van Heijenoort J (October 2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Natural Product Reports. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.