6-oxocamphor hydrolase
| 6-oxocamphor hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.7.1.18 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
6-oxocamphor hydrolase (EC 3.7.1.18, OCH, camK (gene)) is an enzyme with systematic name bornane-2,6-dione hydrolase.[1][2][3] This enzyme catalyses the following chemical reaction
- bornane-2,6-dione + H2O [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate
This enzyme is isolated from Rhodococcus sp.
References
- ↑ Grogan, G.; Roberts, G.A.; Bougioukou, D.; Turner, N.J.; Flitsch, S.L. (2001). "The desymmetrization of bicyclic β-diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily". J. Biol. Chem. 276 (16): 12565–12572. doi:10.1074/jbc.M011538200. PMID 11278926.
- ↑ Whittingham, J.L.; Turkenburg, J.P.; Verma, C.S.; Walsh, M.A.; Grogan, G. (2003). "The 2-Å crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily". J. Biol. Chem. 278 (3): 1744–1750. doi:10.1074/jbc.M211188200. PMID 12421807.
- ↑ Leonard, P.M.; Grogan, G. (2004). "Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-α-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog". J. Biol. Chem. 279: 31312–31317. doi:10.1074/jbc.M403514200. PMID 15138275.
External links
- 6-oxocamphor hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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