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1.1.1.368: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, go to the full flat file.

Reaction

6-hydroxycyclohex-1-ene-1-carbonyl-CoA
+
NAD+
=
6-oxocyclohex-1-ene-1-carbonyl-CoA
+
NADH
+
H+

Synonyms

HAD, ThaADH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.368 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

Substrates Products

Substrates Products on EC 1.1.1.368 - 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-cyclohexanedione + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
-
?
1,3-cyclopentanedione + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
-
?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
show the reaction diagram
additional information
?
-
-
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
-
-
?