Biology: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 | ||||||||
| |||||||||
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 [math]\displaystyle{ \rightleftharpoons }[/math] [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
- "Activation of D-aspartic acid for incorporation into peptidoglycan". J. Biol. Chem. 247 (16): 5095–102. 1972. PMID 4262567.
- "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. 1972. PMID 4626717.
- "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". Protein Sci. 6 (12): 2639–43. 1997. doi:10.1002/pro.5560061218. PMID 9416615.
- "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. 2006. doi:10.1074/jbc.M600114200. PMID 16510449.
 |  |
