6-oxocamphor hydrolase

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

\rightleftharpoons

[(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. and 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. and 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. and 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)

Hydrolases: carbon-carbon (EC 3.7)

3.7.1	Fumarylacetoacetate hydrolase Kynureninase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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