3-hydroxyacyl-CoA dehydrogenase explained
See also: 3-hydroxy-2-methylbutyryl-CoA dehydrogenase.
3-hydroxyacyl-CoA dehydrogenase |
Ec Number: | 1.1.1.35 |
Cas Number: | 9028-40-4 |
Go Code: | 0003857 |
Width: | 270 |
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:
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 .
References
- Hillmer P, Gottschalk G . 1974 . Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri . Biochim. Biophys. Acta . 334 . 12 - 23 . 10.1016/0005-2744(74)90146-6.
- Lehninger AL, Greville GD . The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate . Biochimica et Biophysica Acta . 12 . 1–2 . 188–202 . 1953 . 13115428 . 10.1016/0006-3002(53)90138-3 .
- Stern JR . Crystalline beta-hydroxybutyryl dehydrogenase from pig heart . Biochimica et Biophysica Acta . 26 . 2 . 448–9 . November 1957 . 13499396 . 10.1016/0006-3002(57)90040-9 .
- Wakil SJ, Green DE, Mii S, Mahler HR . Studies on the fatty acid oxidizing system of animal tissues. VI. beta-Hydroxyacyl coenzyme A dehydrogenase . The Journal of Biological Chemistry . 207 . 2 . 631–8 . April 1954 . 10.1016/S0021-9258(18)65679-0 . 13163047 . free .