How Can We Help?
< Back

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) 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:

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 1F0Y, 1F12, 1F14, 1F17, 1F67, 1GZ6, 1IKT, 1IL0, 1LSJ, 1LSO, 1M75, 1M76, 1S9C, 1WDK, 1WDL, 1WDM, 1ZBQ, 1ZCJ, 2D3T, 2HDH, 3HAD, and 3HDH.

References


Categories
Table of Contents