EC Number   |
General Information |
Reference |
|---|
  3.7.1.11 | evolution |
the ring-cleaving cyclohexane-1,2-dione hydrolase is a member of the thiamine diphosphate enzyme family |
-, 719464, 719735 |
| 3.7.1.11 | metabolism |
in the biodegradation pathway of cyclohexane-1,2-diol by Azoarcus sp. strain 22Lin, the last two degradation steps, a biodegradation pathway for alpha-diketones, are catalyzed by cyclohexane-1,2-dione hydrolase |
-, 735301 |
| 3.7.1.11 | more |
enzyme structure and active site structure analysis from the enzyme-substrate complex crystal structure, PDB ID 2PGN |
-, 735301 |
| 3.7.1.11 | more |
the active site funnel is rearranged in an unprecedented manner providing the structural basis for the specific binding and cleavage of an alicyclic compound, including a decreased and displaced funnel entrance, a semicircularly shaped loop segment preceding the C-terminal arm and the attachment of the C-terminal arm to other subunits of the CDH tetramer, asymmetry of the two active sites, architecture of the active site funnel of CDH in comparison with other ThDP dependent enzymes, overview |
-, 719464 |
| 3.7.1.11 | more |
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G |
-, 733089 |
| 3.7.1.11 | physiological function |
CDH catalyses a key step of an anaerobic degradation pathway for alicyclic alcohols by converting cyclohexane-1,2-dione to 6-oxohexanoate and further to adipate using NAD+ as electron acceptor |
-, 719464, 719735 |
| 3.7.1.11 | physiological function |
thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols |
-, 733657 |
