Enzyme

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EC Tree
     3. Hydrolases
        3.7 Acting on carbon-carbon bonds
            3.7.1 In ketonic substances
ID:3.7.1.18
Description:6-oxocamphor hydrolase.
Cath: 3.90.226.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.7.1.18
BRENDA Enzyme Link: BRENDA 3.7.1.18
KEGG Enzyme Link: KEGG3.7.1.18
BioCyc Enzyme Link: BioCyc 3.7.1.18
ExPASy Enzyme Link: ExPASy3.7.1.18
EC2PDB Enzyme Link: EC2PDB 3.7.1.18
ExplorEnz Enzyme Link: ExplorEnz 3.7.1.18
PRIAM enzyme-specific profiles Link: PRIAM 3.7.1.18
IntEnz Enzyme Link: IntEnz 3.7.1.18
MEDLINE Enzyme Link: MEDLINE 3.7.1.18
MSA:

3.7.1.18;

Phylogenetic Tree:

3.7.1.18;

Uniprot:
M-CSA:
RHEA:33415 bornane-2,6-dione + H2O = [(1S)-4-hydroxy-2,2,3-trimethylcyclopent-3-enyl]acetate + H(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[C;H0;+0:4](=[*:5])-[*:6])-[C;H0;+0:7](-[*:8])=[O;H0;+0:9].[OH2;+0:10]>>([*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:7](-[*:8])-[OH;+0:9].[*:5]=[C;H0;+0:4](-[*:6])-[OH;+0:10])
Reaction
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References

TitleAuthorsDatePubMed ID
Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog.Leonard PM, Grogan G2004 Jul 2315138275
The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily.Grogan G, Roberts GA, Bougioukou D, Turner NJ, Flitsch SL2001 Apr 2011278926