3-hydroxyacyl-CoA dehydrogenase
| 3-hydroxyacyl-CoA dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 (S)-3-hydroxybutyryl-CoA dehydrogenase homodimer, Cupriavidus necator | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.35 | ||||||||
| CAS no. | 9028-40-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Hydroxyacyl-Coenzyme A dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
 PDB rendering based on 3had. | |||||||
| Identifiers | |||||||
| Symbol | HADH | ||||||
| Alt. symbols | HADHSC | ||||||
| NCBI gene | 3033 | ||||||
| HGNC | 4799 | ||||||
| OMIM | 601609 | ||||||
| RefSeq | NM_005327 | ||||||
| UniProt | Q16836 | ||||||
| Other data | |||||||
| EC number | 1.1.1.35 | ||||||
| Locus | Chr. 4 q22-q26 | ||||||
| |||||||
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:
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 PDB: 1F0Y, PDB: 1F12, PDB: 1F14, PDB: 1F17, PDB: 1F67, PDB: 1GZ6, PDB: 1IKT, PDB: 1IL0, PDB: 1LSJ, PDB: 1LSO, PDB: 1M75, PDB: 1M76, PDB: 1S9C, PDB: 1WDK, PDB: 1WDL, PDB: 1WDM, PDB: 1ZBQ, PDB: 1ZCJ, PDB: 2D3T, PDB: 2HDH, PDB: 3HAD, and PDB: 3HDH.
See also
- Acetoacetyl-CoA reductase acting on the enantiomer of the substrate
- 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
References
- Hillmer P, Gottschalk G (1974). "Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri". Biochim. Biophys. Acta. 334: 12–23. doi:10.1016/0005-2744(74)90146-6.
- Lehninger AL, Greville GD (1953). "The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate". Biochimica et Biophysica Acta. 12 (1–2): 188–202. doi:10.1016/0006-3002(53)90138-3. PMID 13115428.
- Stern JR (November 1957). "Crystalline beta-hydroxybutyryl dehydrogenase from pig heart". Biochimica et Biophysica Acta. 26 (2): 448–9. doi:10.1016/0006-3002(57)90040-9. PMID 13499396.
- Wakil SJ, Green DE, Mii S, Mahler HR (April 1954). "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. doi:10.1016/S0021-9258(18)65679-0. PMID 13163047.