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| UDP-N-acetylmuramate—L-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.8 | ||||||||
| CAS no. | 9023-52-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a UDP-N-acetylmuramate—L-alanine ligase (EC 6.3.2.8) is an enzyme that catalyzes the chemical reaction
- ATP + UDP-N-acetylmuramate + L-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramate, and L-alanine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanine.
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-acetylmuramate:L-alanine ligase (ADP-forming). Other names in common use include MurC synthetase, UDP-N-acetylmuramoyl-L-alanine synthetase, uridine diphospho-N-acetylmuramoylalanine synthetase, UDP-N-acetylmuramoylalanine synthetase, L-alanine-adding enzyme, UDP-acetylmuramyl-L-alanine synthetase, UDPMurNAc-L-alanine synthetase, L-Ala ligase, uridine diphosphate N-acetylmuramate:L-alanine ligase, uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase, uridine-diphosphate-N-acetylmuramate:L-alanine ligase, UDP-MurNAc:L-alanine ligase, alanine-adding enzyme, and UDP-N-acetylmuramyl:L-alanine ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.
Structural studies
[edit]As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1GQQ, PDB: 1GQY, PDB: 1J6U, PDB: 1P31, PDB: 1P3D, and PDB: 2F00.
See also
[edit]References
[edit]- 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: 2689–2695. doi:10.1016/S0021-9258(19)73808-3.
- Nathenson SG, Strominger JL, Ito, E (1964). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides IV. Purification and properties of D-glutamic acid-adding enzyme". J. Biol. Chem. 239: 1773–1776. doi:10.1016/S0021-9258(18)91256-1. PMID 14213349.
- van Heijenoort J (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 (5): 503–19. doi:10.1039/a804532a. PMID 11699883.
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