Literature summary for 1.1.1.35 extracted from

Xu, Y.; Sun, F.
Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans (2013), Acta Crystallogr. Sect. F, 69, 515-519.

Cloned(Commentary)

Cloned (Comment)	Organism
gene F54C8.1, recombinant expression of C-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3)	Caenorhabditis elegans

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 25 mM sodium acetate trihydrate, pH 5.0, and 300 mM sodium chloride is mixed with an equal volume of reservoir solution, containing 21% PEG 3350, 0.2 M sodium chloride, 0.1 M MES, pH 6.5, for parallelepiped-shaped crystals and 23% PEG 3350, 0.2 M sodium chloride, 0.1 M bicine, pH 8.0, for cuboid-shaped crystals, equilibration against 0.20 ml reservoir solution, 3-5days at 18°C, X-ray diffraction structure determination and analysis of parallelepiped-shaped cuboid-shaped crystal at 1.60 A and 2.20 A resolution, respectively	Caenorhabditis elegans

Crystallization (Comment)

Organism

purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 25 mM sodium acetate trihydrate, pH 5.0, and 300 mM sodium chloride is mixed with an equal volume of reservoir solution, containing 21% PEG 3350, 0.2 M sodium chloride, 0.1 M MES, pH 6.5, for parallelepiped-shaped crystals and 23% PEG 3350, 0.2 M sodium chloride, 0.1 M bicine, pH 8.0, for cuboid-shaped crystals, equilibration against 0.20 ml reservoir solution, 3-5days at 18°C, X-ray diffraction structure determination and analysis of parallelepiped-shaped cuboid-shaped crystal at 1.60 A and 2.20 A resolution, respectively

Caenorhabditis elegans

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial matrix	-	Caenorhabditis elegans	5759	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(S)-3-hydroxyacyl-CoA + NAD+	Caenorhabditis elegans	-	3-oxoacyl-CoA + NADH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Caenorhabditis elegans	P34439	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, cleavage of the GST-tag by PPase, followed by gel filtration, anion exchange chromatography, and ultrafiltration	Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-3-hydroxyacyl-CoA + NAD+	-	Caenorhabditis elegans	3-oxoacyl-CoA + NADH + H+	-	r

Synonyms

Synonyms	Comment	Organism
F54C8.1	-	Caenorhabditis elegans
HAD	-	Caenorhabditis elegans

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Caenorhabditis elegans
NADH	-	Caenorhabditis elegans

General Information

General Information	Comment	Organism
evolution	based on the chain length of the substrates, the HAD family is divided into three subclasses: 3-hydroxyacyl-CoA dehydrogenases (HADs), long-chain 3-hydroxyacyl-CoA dehydrogenases (LCHADs) and short-chain 3-hydroxyacyl-CoA dehydrogenases (SCHADs). HADs are soluble dimeric enzymes that exhibit substrate specificity for an acyl-chain length of C4-C10 and are previously referred to as short-chain HADs	Caenorhabditis elegans
metabolism	3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group	Caenorhabditis elegans