UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase

In enzymology, a 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 ${\displaystyle \rightleftharpoons }$ ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase
Identifiers
EC no.	6.3.2.7
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

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: 2689–2695.
• 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.