D-alanine-D-alanine ligase

From Wikipedia, the free encyclopedia

In enzymology, a D-alanine-D-alanine ligase (EC 6.3.2.4) is an enzyme that catalyzes the chemical reaction

ATP + 2 D-alanine $\rightleftharpoons$ ADP + phosphate + D-alanyl-D-alanine

Thus, the two substrates of this enzyme are ATP and D-alanine, whereas its 3 products are ADP, phosphate, and 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). The systematic name of this enzyme class is D-alanine:D-alanine ligase (ADP-forming). Other names in common use include MurE synthetase [ambiguous], alanine:alanine ligase (ADP-forming), and alanylalanine synthetase. This enzyme participates in d-alanine metabolism and peptidoglycan biosynthesis. At least one compound, Phosphinate is known to inhibit this enzyme.

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

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1EHI, 1IOV, 1IOW, 2DLN, 2FB9, 2I80, 2I87, and 2I8C.

[edit] References

IUBMB entry for 6.3.2.4
BRENDA references for 6.3.2.4 (Recommended.)
PubMed references for 6.3.2.4
PubMed Central references for 6.3.2.4
Google Scholar references for 6.3.2.4
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.
Neuhaus FC (1962). "Kinetic studies on D-Ala-D-Ala synthetase". Fed. Proc. 21: 229.
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.