UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase
| UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.10 | ||||||||
| CAS no. | 9023-60-3 | ||||||||
| 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, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase (EC 6.3.2.10) is an enzyme that catalyzes the chemical reaction
- ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- alanine
The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine, and D-alanyl-D-alanine, whereas its 4 products are ADP, phosphate, UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-, and alanine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).
Nomenclature[edit]
The systematic name of this enzyme class is UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine:D-alanyl-D-alanine ligase (ADP-forming). Other names in common use include MurF synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, synthetase, UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine, ligase, uridine diphosphoacetylmuramoylpentapeptide synthetase, UDPacetylmuramoylpentapeptide synthetase, and UDP-MurNAc-L-Ala-D-Glu-L-Lys:D-Ala-D-Ala ligase. This enzyme participates in lysine biosynthesis and peptidoglycan biosynthesis.
References[edit]
- Ito E, Strominger JL (1962). "Enzymatic synthesis of the peptide in bacterial uridine nucleotides II. Enzymatic synthesis and addition of D-alanyl-D-alanine". J. Biol. Chem. 237: 2696–2703.
- 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.
