UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase

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In enzymology, an 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 $\rightleftharpoons$ 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-, and 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-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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2AM1 and 2AM2.

[edit] References

IUBMB entry for 6.3.2.10
BRENDA references for 6.3.2.10 (Recommended.)
PubMed references for 6.3.2.10
PubMed Central references for 6.3.2.10
Google Scholar references for 6.3.2.10
Ito, E and 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.
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.