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
| Clavaminate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.21 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- (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 edit
- ^ Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA (February 1991). "Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction". Biochemistry. 30 (8): 2281–92. 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, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ (February 2000). "Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase". Nature Structural Biology. 7 (2): 127–33. doi:10.1038/72398. PMID 10655615.
- ^ Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI (August 2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities". Journal of the American Chemical Society. 123 (30): 7388–98. doi:10.1021/ja004025+. PMID 11472170.
- ^ Townsend CA (October 2002). "New reactions in clavulanic acid biosynthesis". Current Opinion in Chemical Biology. 6 (5): 583–9. doi:10.1016/S1367-5931(02)00392-7. PMID 12413541.
External links edit
- Clavaminate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
