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

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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 $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 6.3.2.7
BRENDA references for 6.3.2.7 (Recommended.)
PubMed references for 6.3.2.7
PubMed Central references for 6.3.2.7
Google Scholar references for 6.3.2.7
Ito, E and 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 (2001). "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18: 503–19. doi:10.1039/a804532a. PMID 11699883.