Application | Comment | Organism |
---|---|---|
diagnostics | the enzyme is a useful marker in the assay of diabetes mellitus and/or ketoacidosis | Alcaligenes faecalis |
Cloned (Comment) | Organism |
---|---|
enzyme expression in Escherichia coli strain DH1 | Alcaligenes faecalis |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-3-hydroxybutanoate + NAD+ | Alcaligenes faecalis | - |
acetoacetate + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | D0VWQ0 | - |
- |
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 | 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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-3-hydroxybutanoate + NAD+ | - |
Alcaligenes faecalis | acetoacetate + NADH | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | secondary and tertiary enzyme structure analysis, overview | Alcaligenes faecalis |
Synonyms | Comment | Organism |
---|---|---|
D-3-hydroxybutyrate dehydrogenase | - |
Alcaligenes faecalis |
HBDH | - |
Alcaligenes faecalis |
More | the enzyme belongs to the SDR family | Alcaligenes faecalis |
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 |