Clavaminate synthase
| Clavaminate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.21 | ||||||||
| CAS number | 122799-56-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating).[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- (1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2 amidinoproclavaminate + succinate + CO2
- (2) proclavaminate + 2-oxoglutarate + O2 dihydroclavaminate + succinate + CO2 + H2O
- (3) dihydroclavaminate + 2-oxoglutarate + O2 clavaminate + succinate + CO2 + H2O
Clavaminate synthase contains nonheme iron.
References
- ↑ Salowe, S.P.; Krol, W.J.; Iwatareuyl, D.; Townsend, C.A. (1991). "Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction". Biochemistry. 30 (8): 2281–2292. doi:10.1021/bi00222a034. PMID 1998687.
- ↑ Zhou, J.; Gunsior, M.; Bachmann, B.O.; Townsend, C.A.; Solomon, E.I. (1998). "Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation". J. Am. Chem. Soc. 120: 13539–13540. doi:10.1021/ja983534x.
- ↑ Zhang, Z.H.; Ren, J.S.; Stammers, D.K.; Baldwin, J.E.; Harlos, K.; Schofield, C.J. (2000). "Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase". Nat. Struct. Biol. 7 (2): 127–133. doi:10.1038/72398. PMID 10655615.
- ↑ Zhou, J.; Kelly, W.L.; Bachmann, B.O.; Gunsior, M.; Townsend, C.A.; Solomon, E.I. (2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities". J. Am. Chem. Soc. 123: 7388–7398. doi:10.1021/ja004025. PMID 11472170.
- ↑ Townsend, C.A. (2002). "New reactions in clavulanic acid biosynthesis". Curr. Opin. Chem. Biol. 6: 583–589. doi:10.1016/S1367-5931(02)00392-7. PMID 12413541.
External links
- Clavaminate synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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