EC number:6.1.2.1
Enzyme
Download| EC Tree |
| 6. Ligases |
| 6.1 Forming carbon-oxygen bonds |
| 6.1.2 acid-alcohol ligases (ester synthases) |
| ID: | 6.1.2.1 |
|---|---|
| Description: | D-alanine--(R)-lactate ligase. |
| Cath: | 3.30.1490.20; 3.30.470.20; 3.40.50.20; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 6.1.2.1 |
| BRENDA Enzyme Link: | BRENDA 6.1.2.1 |
| KEGG Enzyme Link: | KEGG6.1.2.1 |
| BioCyc Enzyme Link: | BioCyc 6.1.2.1 |
| ExPASy Enzyme Link: | ExPASy6.1.2.1 |
| EC2PDB Enzyme Link: | EC2PDB 6.1.2.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.1.2.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.1.2.1 |
| IntEnz Enzyme Link: | IntEnz 6.1.2.1 |
| MEDLINE Enzyme Link: | MEDLINE 6.1.2.1 |
| RHEA:37347 | (R)-lactate + ATP + D-alanine = ADP + D-alanyl-(R)-lactate + phosphate |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:1]-[O;H0;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:12]-[OH;+0:11].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| VanD-type glycopeptide-resistant Enterococcus faecium BM4339. | Perichon B, Reynolds P, Courvalin P | 1997 Sep | 9303405 |
| Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583. | Meziane-Cherif D, Badet-Denisot MA, Evers S, Courvalin P, Badet B | 1994 Nov 7 | 7957913 |
| Role of Arg301 in substrate orientation and catalysis in subsite 2 of D-alanine:D-alanine (D-lactate) ligase from Leuconostoc mesenteroides: a molecular docking study. | Neuhaus FC | 2010 Jun | 20167520 |