D-aspartate ligase

D-aspartate ligase
Identifiers
EC number	6.3.1.12
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles

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 $\rightleftharpoons$ [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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2143612. 
• 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. 

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