Literature summary for 1.1.1.35 extracted from

Kim, J.; Kim, K.
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha H16 (2014), Acta Crystallogr. Sect. F, 70, 955-958.

Application

Application	Comment	Organism
synthesis	the enzyme is used in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to (S)-3-hydroxybutyryl-CoA	Cupriavidus necator

Cloned(Commentary)

Cloned (Comment)	Organism
gene paaH1, recombinant expression of C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes in Escherichia coli strain B834	Cupriavidus necator

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 30 mg/ml wild-type protein or 25 mg/ml selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.0, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion method	Cupriavidus necator

Crystallization (Comment)

Organism

purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 30 mg/ml wild-type protein or 25 mg/ml selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.0, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion method

Cupriavidus necator

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(S)-3-hydroxybutanoyl-CoA + NAD+	Cupriavidus necator	-	acetoacetyl-CoA + NADH + H+	-	r
(S)-3-hydroxybutanoyl-CoA + NAD+	Cupriavidus necator ATCC 17699	-	acetoacetyl-CoA + NADH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	Q0KEY8	-	-
Cupriavidus necator ATCC 17699	Q0KEY8	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration	Cupriavidus necator

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-3-hydroxybutanoyl-CoA + NAD+	-	Cupriavidus necator	acetoacetyl-CoA + NADH + H+	-	r
(S)-3-hydroxybutanoyl-CoA + NAD+	-	Cupriavidus necator ATCC 17699	acetoacetyl-CoA + NADH + H+	-	r

Synonyms

Synonyms	Comment	Organism
(S)-3-hydroxybutyryl-CoA dehydrogenase	-	Cupriavidus necator
PaaH1	-	Cupriavidus necator

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Cupriavidus necator
NADH	-	Cupriavidus necator

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA	Cupriavidus necator