ATP + UDP-N-acetylmuramoyl-L-alanine + D-glutamate $rightleftharpoons$ ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate

The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramoyl-L-alanine, and D-glutamate, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanyl-D-glutamate.

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-alanine:D-glutamate ligase (ADP-forming). Other names in common use include MurD synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamate synthetase, D-glutamate-adding enzyme, D-glutamate ligase, UDP-Mur-NAC-L-Ala:D-Glu ligase, UDP-N-acetylmuramoyl-L-alanine:glutamate ligase (ADP-forming), and UDP-N-acetylmuramoylalanine-D-glutamate ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .

References

• Ito, E and Strominger JL "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 "Recent advances in the formation of the bacterial peptidoglycan monomer unit". Nat. Prod. Rep. 18 503–19.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes