EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   1.1.1.368 | 1,2-cyclohexanedione + NADH + H+ |
- |
Thauera aromatica |
? + NAD+ |
- |
? |
| 1.1.1.368 | 1,3-cyclopentanedione + NADH + H+ |
- |
Thauera aromatica |
? + NAD+ |
- |
? |
| 1.1.1.368 | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ |
- |
Thauera aromatica |
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+ |
- |
? |
| 1.1.1.368 | more |
the enzyme exhibits a substrate specificity with highest activities on cyclic alpha- and beta-diketones including 1,2-cyclohexanedione and 1,3-cyclopentanedione, enzyme activity with 1,2-cyclohexanedione, 1,3-cyclohexanedione, and 1,3-cyclopentanedione as well as with 2,3/pentanedione, ethyl pyruvate, and cyclohexanone, but ThaADH converts neither acetophenone nor benzaldehyde which are both preferred substrates of many known zinc-dependent ADHs. The enzyme actually prefers substrates with the reactive carbonyl function being located inside a cyclohexyl or cyclopentyl structure |
Thauera aromatica |
? |
- |
? |
| 1.1.1.368 | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ |
the enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria |
Thauera aromatica |
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+ |
- |
ir |
| 1.1.1.368 | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ |
the enzyme is specific for NAD+, no activity with NADP+. The enzyme is specific for 6-hydroxycyclohex-1-ene-1-carbonyl-CoA, no activity with 2-hydroxycyclohexane-1-carbonyl-CoA |
Thauera aromatica |
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+ |
- |
ir |
