In enzymology, a D-aspartate ligase ( EC 6.3.1.12) is an enzyme that catalyzes the chemical reaction

ATP + D-aspartate + [beta-GlcNAc-(1->4)-Mur₂Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D- Ala)]n ${\displaystyle \rightleftharpoons }$ [beta-GlcNAc-(1->4)-Mur₂Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L- Lys-D-Ala-D-Ala)]n + ADP + phosphate

The 4 substrates of this enzyme are ATP, D-aspartate, [[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-]], and [[Ala)]n]], whereas its 4 products are [[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-]], [[Lys-D-Ala-D-Ala)]n]], ADP, and phosphate.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). The systematic name of this enzyme class is D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D -Ala-D-Ala)]n ligase (ADP-forming). Other names in common use include Aslfm, UDP-MurNAc-pentapeptide:D-aspartate ligase, and D-aspartic acid-activating enzyme.

References

• Staudenbauer W, Strominger JL (1972). "Activation of D-aspartic acid for incorporation into peptidoglycan". J. Biol. Chem. 247 (16): 5095–102. PMID  4262567.
• Staudenbauer W, Willoughby E, Strominger JL (1972). "Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane". J. Biol. Chem. 247 (17): 5289–96. PMID  4626717.
• Galperin MY, Koonin EV (1997). "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". Protein Sci. 6 (12): 2639–43. doi: 10.1002/pro.5560061218. PMC  2143612. PMID  9416615.
• Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL (2006). "Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium". J. Biol. Chem. 281 (17): 11586–94. doi: 10.1074/jbc.M600114200. PMID  16510449.