UDP-N-acetylmuramate—L-alanine ligase explained

UDP-N-acetylmuramate—L-alanine ligase
Ec Number:	6.3.2.8
Cas Number:	9023-52-3
Go Code:	0008763

In enzymology, a UDP-N-acetylmuramate—L-alanine ligase is an enzyme that catalyzes the chemical reaction

ATP + UDP-N-acetylmuramate + L-alanine

\rightleftharpoons ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine

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

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-acetylmuramate:L-alanine ligase (ADP-forming). Other names in common use include MurC synthetase, UDP-N-acetylmuramoyl-L-alanine synthetase, uridine diphospho-N-acetylmuramoylalanine synthetase, UDP-N-acetylmuramoylalanine synthetase, L-alanine-adding enzyme, UDP-acetylmuramyl-L-alanine synthetase, UDPMurNAc-L-alanine synthetase, L-Ala ligase, uridine diphosphate N-acetylmuramate:L-alanine ligase, uridine 5'-diphosphate-N-acetylmuramyl-L-alanine synthetase, uridine-diphosphate-N-acetylmuramate:L-alanine ligase, UDP-MurNAc:L-alanine ligase, alanine-adding enzyme, and UDP-N-acetylmuramyl:L-alanine ligase. This enzyme participates in d-glutamine and d-glutamate metabolism and peptidoglycan biosynthesis.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes,,,,, and .

See also

• Muramyl ligase

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 .
• Nathenson SG, Strominger JL, Ito, E . 1964 . Enzymatic synthesis of the peptide in bacterial uridine nucleotides IV. Purification and properties of D-glutamic acid-adding enzyme . J. Biol. Chem. . 239 . 1773 - 1776 . 14213349.
• van Heijenoort J . 2001 . Recent advances in the formation of the bacterial peptidoglycan monomer unit . Nat. Prod. Rep. . 18 . 503 - 19 . 11699883 . 10.1039/a804532a . 5 .