EC number:6.3.3.6
| ID: | 6.3.3.6 |
|---|---|
| Description: | Carbapenam-3-carboxylate synthase. |
| Alternative Name: |
Carbapenam-3-carboxylate ligase. |
| Cath: | 3.40.50.620; 3.60.20.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 6.3.3.6 |
| BRENDA Enzyme Link: | BRENDA 6.3.3.6 |
| KEGG Enzyme Link: | KEGG6.3.3.6 |
| BioCyc Enzyme Link: | BioCyc 6.3.3.6 |
| ExPASy Enzyme Link: | ExPASy6.3.3.6 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.3.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.3.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.3.6 |
| IntEnz Enzyme Link: | IntEnz 6.3.3.6 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.3.6 |
| RHEA:36703 | (2S,5S)-5-carboxymethylproline + ATP = (3S,5S)-carbapenam-3-caboxylate + AMP + diphosphate + H(+) |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:7]=[C;H0;+0:8](-[OH;+0:9])-[*:10]-[*:11]-[NH;+0:12]-[*:13]>>[*:1]-[OH;+0:2].[*:4]-[P;H0;+0:3](=[*:5])(-[*:6])-[OH;+0:9].[*:7]=[C;H0;+0:8]1-[*:10]-[*:11]-[N;H0;+0:12]-1-[*:13] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes: carbapenam synthetase and beta-lactam synthetase. | Raber ML, Arnett SO, Townsend CA | 2009 Jun 9 | 19371088 |
| Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase. | Arnett SO, Gerratana B, Townsend CA | 2007 Aug 14 | 17658887 |
| Crystal structure of carbapenam synthetase (CarA). | Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC | 2003 Oct 17 | 12890666 |
| Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora. | Gerratana B, Stapon A, Townsend CA | 2003 Jul 1 | 12820893 |