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 .
See also Acetoacetyl-CoA reductase acting on the enantiomer of the substrate 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
References