Literature summary for 1.1.1.30 extracted from

Hoque, M.M.; Shimizu, S.; Hossain, M.T.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Tsunoda, M.; Amano, H.; Sekiguchi, T.; Takenaka, A.
The structures of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase before and after NAD+ and acetate binding suggest a dynamical reaction mechanism as a member of the SDR family (2008), Acta Crystallogr. Sect. D, 64, 496-505.

Search for more literature for 1.1.1.30

Application

Application	Comment	Organism
diagnostics	the enzyme is a useful marker in the assay of diabetes mellitus and/or ketoacidosis	Alcaligenes faecalis

Cloned(Commentary)

Cloned (Comment)	Organism
enzyme expression in Escherichia coli strain DH1	Alcaligenes faecalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of the enzyme in the apo form and in the holo form with acetate as a substrate analogue, method screening, mother liquor consists of 30% w/v PEG 4000, 0.2 M sodium acetate trihydrate and 100 mM Tris-HCl, pH 8.5, at 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular-replacement method	Alcaligenes faecalis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(R)-3-hydroxybutanoate + NAD+	Alcaligenes faecalis	-	acetoacetate + NADH	-	r

Organism

Organism	UniProt	Comment	Textmining
Alcaligenes faecalis	D0VWQ0	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain DH1 by anion exchange chromatography, hydrophobic interaction chromatography using a gradient of 1-20% ammonium sulfate, and ultrafiltration	Alcaligenes faecalis

Reaction

Reaction	Comment	Organism	Reaction ID
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+	the enzyme shows a dynamical reaction mechanism. In the catalytic site, a water molecule is trapped by the catalytic Tyr155 and Ser142 residues in the vicinity of the bound NAD+ and acetate, substrate binding structure, overview	Alcaligenes faecalis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-3-hydroxybutanoate + NAD+	-	Alcaligenes faecalis	acetoacetate + NADH	-	r

Subunits

Subunits	Comment	Organism
More	secondary and tertiary enzyme structure analysis, overview	Alcaligenes faecalis

Synonyms

Synonyms	Comment	Organism
D-3-hydroxybutyrate dehydrogenase	-	Alcaligenes faecalis
HBDH	-	Alcaligenes faecalis
More	the enzyme belongs to the SDR family	Alcaligenes faecalis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	NAD+ is bound in a large cleft in the domain. The diphosphate group of NAD+ is covered by the small additional domain, which is supported by two extended arms allowing domain movement	Alcaligenes faecalis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)