EC number:6.3.3.4
| ID: | 6.3.3.4 |
|---|---|
| Description: | (Carboxyethyl)arginine beta-lactam-synthase. |
| Alternative Name: |
Beta-lactam synthetase. |
| Cath: | 3.40.50.620; 3.60.20.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 6.3.3.4 |
| BRENDA Enzyme Link: | BRENDA 6.3.3.4 |
| KEGG Enzyme Link: | KEGG6.3.3.4 |
| BioCyc Enzyme Link: | BioCyc 6.3.3.4 |
| ExPASy Enzyme Link: | ExPASy6.3.3.4 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.3.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.3.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.3.4 |
| IntEnz Enzyme Link: | IntEnz 6.3.3.4 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.3.4 |
| RHEA:23620 | ATP + N(2)-(2-carboxyethyl)-L-arginine = AMP + deoxyamidinoproclavaminate + 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 | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| New reactions in clavulanic acid biosynthesis. | Townsend CA | 2002 Oct | 12413541 |
| Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities. | Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI | 2001 Aug 1 | 11472170 |
| The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots. | Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC | 2002 Nov 12 | 12409610 |
| Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine. | Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC | 2001 Aug | 11473258 |
| Kinetic mechanism of the beta-lactam synthetase of Streptomyces clavuligerus. | Bachmann BO, Townsend CA | 2000 Sep 19 | 10985764 |