| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases) |
| ID: | 6.3.1.12 | ||
|---|---|---|---|
| Description: | D-aspartate ligase. | ||
| Alternative Name: |
D-aspartic acid-activating enzyme. Asl(fm). | ||
| Prosite: | PDOC50975; | ||
| PDB: |
|
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 6.3.1.12 |
| BRENDA Enzyme Link: | BRENDA 6.3.1.12 |
| KEGG Enzyme Link: | KEGG6.3.1.12 |
| BioCyc Enzyme Link: | BioCyc 6.3.1.12 |
| ExPASy Enzyme Link: | ExPASy6.3.1.12 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.1.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.1.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.1.12 |
| IntEnz Enzyme Link: | IntEnz 6.3.1.12 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.1.12 |
| RHEA:10752 | [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n) + n ATP + n D-aspartate = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n H(+) + n phosphate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. | Galperin MY, Koonin EV | 1997 Dec | 9416615 |
| Further studies of the D-aspartic acid-activating enzyme of Streptococcus faecalis and its attachment to the membrane. | Staudenbauer W, Willoughby E, Strominger JL | 1972 Sep 10 | 4626717 |
| Activation of D-aspartic acid for incorporation into peptidoglycan. | Staudenbauer W, Strominger JL | 1972 Aug 25 | 4262567 |
| Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium. | Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL | 2006 Apr 28 | 16510449 |