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Literature summary 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.
    View publication on PubMed

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.30 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.30 Alcaligenes faecalis D0VWQ0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.30 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

EC Number Reaction Comment Organism Reaction ID
1.1.1.30 (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)

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

Subunits

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.30 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