EC |
3.7.1.18 |
Accepted name: |
6-oxocamphor hydrolase |
Reaction: |
bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate |
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For diagram of camphor catabolism, click here |
Glossary: |
α-campholonate = (4-hydroxy-2,2,3-trimethylcyclopent-3-enyl)acetate (enol form) = (2,2,3-trimethyl-4-oxocyclopentyl)acetate (keto form) |
Other name(s): |
OCH; camK (gene name) |
Systematic name: |
bornane-2,6-dione hydrolase |
Comments: |
Isolated from Rhodococcus sp. The bornane ring system is cleaved by a retro-Claisen reaction to give the enol of α-campholonate. When separate from the enzyme the enol is tautomerised to the keto form as a 6:1 mixture of [(1S,3R)-2,2,3-trimethyl-4-oxocyclopentyl]acetate and [(1S,3S)-2,2,3-trimethyl-4-oxocyclopentyl]acetate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Grogan, G., Roberts, G.A., Bougioukou, D., Turner, N.J. and Flitsch, S.L. The desymmetrization of bicyclic β-diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily. J. Biol. Chem. 276 (2001) 12565–12572. [DOI] [PMID: 11278926] |
2. |
Whittingham, J.L., Turkenburg, J.P., Verma, C.S., Walsh, M.A. and Grogan, G. The 2-Å crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily. J. Biol. Chem. 278 (2003) 1744–1750. [DOI] [PMID: 12421807] |
3. |
Leonard, P.M. and Grogan, G. 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 (2004) 31312–31317. [DOI] [PMID: 15138275] |
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[EC 3.7.1.18 created 2012] |
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