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 ⇌ {\displaystyle \rightleftharpoons } 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-alanine. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).
Nomenclature 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
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. doi:10.1016/S0021-9258(19)73809-5. 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.
