In enzymology, a 3-hydroxyacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
(S)-3-hydroxyacyl-CoA + NAD+ 3-oxoacyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD+, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.
Isozymes
In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity: HADH – Hydroxyacyl-Coenzyme A dehydrogenase HSD17B10 – 3-Hydroxyacyl-CoA dehydrogenase type-2 EHHADH – Peroxisomal bifunctional enzyme HSD17B4 – Peroxisomal multifunctional enzyme type 2
Function
3-Hydroxyacyl CoA dehydrogenase is classified as an oxidoreductase. It is involved in fatty acid metabolic processes. Specifically it catalyzes the third step of beta oxidation; the oxidation of L-3-hydroxyacyl CoA by NAD+. The reaction converts the hydroxyl group into a keto group.
The end product is 3-ketoacyl CoA.
Metabolic pathways
This enzyme participates in 8 metabolic pathways:
fatty acid elongation in mitochondria
fatty acid metabolism
valine, leucine and isoleucine degradation
lysine degradation
tryptophan metabolism
benzoate degradation via coa ligation
butanoate metabolism
caprolactam degradation
Nomenclature
The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase. Other names in common use include:
1-specific DPN-linked beta-hydroxybutyric dehydrogenase
3-hydroxyacetyl-coenzyme A dehydrogenase
3-hydroxyacyl coenzyme A dehydrogenase
3-hydroxybutyryl-CoA dehydrogenase
3-hydroxyisobutyryl-CoA dehydrogenase
3-keto reductase
3-L-hydroxyacyl-CoA dehydrogenase
3beta-hydroxyacyl coenzyme A dehydrogenase
beta-hydroxy acid dehydrogenase
beta-hydroxyacyl CoA dehydrogenase
beta-hydroxyacyl dehydrogenase
beta-hydroxyacyl-coenzyme A synthetase
beta-hydroxyacylcoenzyme A dehydrogenase
beta-hydroxybutyrylcoenzyme A dehydrogenase
beta-keto-reductase
beta-ketoacyl-CoA reductase
L-3-hydroxyacyl CoA dehydrogenase
L-3-hydroxyacyl coenzyme A dehydrogenase
Structural studies
As of 20 January 2010, 22 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , and .