View source for 3alpha(or 20beta)-hydroxysteroid dehydrogenase

{{See also|3-hydroxy-2-methylbutyryl-CoA dehydrogenase}}
{{enzyme
| Name = 3-hydroxyacyl-CoA dehydrogenase
| EC_number = 1.1.1.35
| CAS_number = 9028-40-4
| IUBMB_EC_number = 1/1/1/35
| GO_code = 0003857
| image = 
| width = 
| caption = 
}}
{{protein
|Name=[[Hydroxyacyl-Coenzyme A dehydrogenase]]
|caption=[[Protein_Data_Bank|PDB]] rendering based on 3had.
|image= PDB_3had_EBI.jpg
|width=
|HGNCid=4799
|Symbol=[[Hydroxyacyl-Coenzyme A dehydrogenase|HADH]]
|AltSymbols=HADHSC
|EntrezGene=3033
|OMIM=601609
|RefSeq=NM_005327
|UniProt=Q16836
|PDB=
|ECnumber=1.1.1.35
|Chromosome=4
|Arm=q
|Band=22
|LocusSupplementaryData=-q26
}}
In [[enzymology]], a '''3-hydroxyacyl-CoA dehydrogenase''' ({{EC number|1.1.1.35}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:(S)-3-hydroxyacyl-CoA + NAD<sup>+</sup> <math>\rightleftharpoons</math> 3-oxoacyl-CoA + NADH + H<sup>+</sup>

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[(S)-3-hydroxyacyl-CoA]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[3-oxoacyl-CoA]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]].

This enzyme belongs to the family of [[oxidoreductase]]s, to be specific those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor.

== Isozymes ==

In humans, the following genes encode proteins with 3-hydroxyacyl-CoA dehydrogenase activity:
* [[Hydroxyacyl-Coenzyme A dehydrogenase|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<sup>+</sup>. The reaction converts the [[hydroxyl]] group into a [[ketone|keto]] group.
[[Image:FattyAcid-MB-OxidationByNAD.png|center]]

The end product is '''3-ketoacyl CoA'''.

== Metabolic pathways ==

This enzyme participates in 8 [[metabolism|metabolic pathways]]:
{{div col|colwidth=30em}}
* [[Fatty acid synthesis|fatty acid elongation in mitochondria]]
* [[fatty acid metabolism]]
* [[valine, leucine and isoleucine degradation]]
* [[lysine degradation]]
* [[tryptophan metabolism]]
* [[benzoate degradation via coa ligation]]
* [[butanoate metabolism]]
* [[caprolactam degradation]]
{{Div col end}}

== Nomenclature ==

The systematic name of this enzyme class is (S)-3-hydroxyacyl-CoA:NAD<sup>+</sup> oxidoreductase. Other names in common use include:
{{div col|colwidth=30em}}
* 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
{{Div col end}}

== Structural studies ==

As of 20 January 2010, 22 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1F0Y}}, {{PDB link|1F12}}, {{PDB link|1F14}}, {{PDB link|1F17}}, {{PDB link|1F67}}, {{PDB link|1GZ6}}, {{PDB link|1IKT}}, {{PDB link|1IL0}}, {{PDB link|1LSJ}}, {{PDB link|1LSO}}, {{PDB link|1M75}}, {{PDB link|1M76}}, {{PDB link|1S9C}}, {{PDB link|1WDK}}, {{PDB link|1WDL}}, {{PDB link|1WDM}}, {{PDB link|1ZBQ}}, {{PDB link|1ZCJ}}, {{PDB link|2D3T}}, {{PDB link|2HDH}}, {{PDB link|3HAD}}, and {{PDB link|3HDH}}.

== References ==
{{reflist|1}}
{{refbegin}}
* {{cite journal | author = Hillmer P and Gottschalk G | date = 1974 | title = Solubilization and partial characterisation of particulate dehydrogenases from ''Clostridium kluyveri'' | journal = Biochim. Biophys. Acta | volume = 334 | pages = 12&ndash;23 }}
* {{cite journal | author = Lehninger AL, Greville GD | title = The enzymic oxidation of alpha- and 2-beta-hydroxybutyrate | journal = Biochim. Biophys. Acta | volume = 12 | issue = 1-2 | pages = 188–202 | year = 1953 | pmid = 13115428 | doi = 10.1016/0006-3002(53)90138-3 | url = | issn = }}
* {{cite journal | author = Stern JR | title = Crystalline beta-hydroxybutyryl dehydrogenase from pig heart | journal = Biochim. Biophys. Acta | volume = 26 | issue = 2 | pages = 448–9 |date=November 1957 | pmid = 13499396 | doi = 10.1016/0006-3002(57)90040-9 | url = | issn = }}
* {{cite journal | author = Wakil SJ, Green DE, Mii S and Mahler HR | title = Studies on the fatty acid oxidizing system of animal tissues. VI. beta-Hydroxyacyl coenzyme A dehydrogenase | journal = J. Biol. Chem. | volume = 207 | issue = 2 | pages = 631–8 |date=April 1954 | pmid = 13163047 | doi = | url = | issn = }}
{{refend}}

{{Alcohol oxidoreductases}}
{{Lipid metabolism enzymes}}

[[Category:EC 1.1.1]]
[[Category:NADH-dependent enzymes]]
[[Category:Enzymes of known structure]]


{{1.1.1-enzyme-stub}}