EC number:1.14.11.21
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor |
| ID: | 1.14.11.21 |
|---|---|
| Description: | Clavaminate synthase. |
| Alternative Name: |
Clavaminic acid synthase. |
| Cath: | 3.40.800.10; 3.60.130.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.11.21 |
| BRENDA Enzyme Link: | BRENDA 1.14.11.21 |
| KEGG Enzyme Link: | KEGG1.14.11.21 |
| BioCyc Enzyme Link: | BioCyc 1.14.11.21 |
| ExPASy Enzyme Link: | ExPASy1.14.11.21 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.11.21 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.21 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.21 |
| IntEnz Enzyme Link: | IntEnz 1.14.11.21 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.11.21 |
EC number:1.14.11.21
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:12773 | 2-oxoglutarate + O2 + proclavaminate = CO2 + dihydroclavaminate + H2O + succinate |
| RULE(radius=1) | ([*:1]-[CH2;+0:2]-[*:3].[*:4]-[OH;+0:5]).[*:6]=[C;H0;+0:7](-[OH;+0:8])-[C;H0;+0:9](=[*:10])-[*:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:4]-[O;H0;+0:5]-[CH;+0:2](-[*:1])-[*:3].[*:10]=[C;H0;+0:9](-[*:11])-[OH;+0:12].[*:6]=[C;H0;+0:7]=[O;H0;+0:8].[OH2;+0:13] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. | Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA | 1991 Feb 26 | 1998687 |
| New reactions in clavulanic acid biosynthesis. | Townsend CA | 2002 Oct | 12413541 |
| Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements. | Zhang Z, Ren Js, Harlos K, McKinnon CH, Clifton IJ, Schofield CJ | 2002 Apr 24 | 12062399 |
| 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 |
| Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase. | Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ | 2000 Feb | 10655615 |
| RHEA:19785 | 2-oxoglutarate + dihydroclavaminate + O2 = clavaminate + CO2 + H2O + succinate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[CH2;+0:4]-[*:5].[*:6]=[C;H0;+0:7](-[OH;+0:8])-[C;H0;+0:9](=[*:10])-[*:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[*:10]=[C;H0;+0:9](-[*:11])-[OH;+0:12].[*:6]=[C;H0;+0:7]=[O;H0;+0:8].[OH2;+0:13] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. | Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA | 1991 Feb 26 | 1998687 |
| New reactions in clavulanic acid biosynthesis. | Townsend CA | 2002 Oct | 12413541 |
| Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements. | Zhang Z, Ren Js, Harlos K, McKinnon CH, Clifton IJ, Schofield CJ | 2002 Apr 24 | 12062399 |
| 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 |
| Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase. | Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ | 2000 Feb | 10655615 |
| RHEA:20021 | 2-oxoglutarate + deoxyamidinoproclavaminate + O2 = amidinoproclavaminate + CO2 + succinate |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. | Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA | 1991 Feb 26 | 1998687 |
| New reactions in clavulanic acid biosynthesis. | Townsend CA | 2002 Oct | 12413541 |
| Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements. | Zhang Z, Ren Js, Harlos K, McKinnon CH, Clifton IJ, Schofield CJ | 2002 Apr 24 | 12062399 |
| 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 |
| Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase. | Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ | 2000 Feb | 10655615 |