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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
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins
Hydroxyacyl-Coenzyme A dehydrogenase
PDB rendering based on 3had.
Identifiers
Symbol HADH
Alt. symbolsHADHSC
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
Search for
Structures Swiss-model
Domains InterPro

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

  • 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.