Refine search

Search Substrates and Products (Substrate)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 6 of 6
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
1,2-cyclohexanedione + NADH + H+
-
? + NAD+
-
?
1,3-cyclopentanedione + NADH + H+
-
? + NAD+
-
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
-
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
-
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
the enzyme participates in the central benzoyl-CoA degradation pathway of some anaerobic bacteria
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
-
ir
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
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
-
ir
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
?
-
-
Results 1 - 6 of 6