ID: | 3.7.1.18 |
---|---|
Description: | 6-oxocamphor hydrolase. |
Cath: | 3.90.226.10; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed 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 G | 2004 Jul 23 | 15138275 |
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 SL | 2001 Apr 20 | 11278926 |