3-hydroxyacyl-CoA dehydrogenase

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