3-hydroxyacyl-CoA dehydrogenase

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3-hydroxyacyl-CoA dehydrogenase
Identifiers
EC number 1.1.1.35
CAS number 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 / EGO
Hydroxyacyl-Coenzyme A dehydrogenase
PDB 3had EBI.jpg
PDB rendering based on 3had.
Identifiers
Symbol HADH
Alt. symbols HADHSC
Entrez 3033
HUGO 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+ \rightleftharpoons 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[edit]

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[edit]

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.

FattyAcid-MB-OxidationByNAD.png

The end product is 3-ketoacyl CoA.

Metabolic pathways[edit]

This enzyme participates in 8 metabolic pathways:

Nomenclature[edit]

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[edit]

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[edit]

  • Hillmer P and 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". Biochim. Biophys. 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". Biochim. Biophys. Acta 26 (2): 448–9. doi:10.1016/0006-3002(57)90040-9. PMID 13499396. 
  • Wakil SJ, Green DE, Mii S and Mahler HR (April 1954). "Studies on the fatty acid oxidizing system of animal tissues. VI. beta-Hydroxyacyl coenzyme A dehydrogenase". J. Biol. Chem. 207 (2): 631–8. PMID 13163047.