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Literature summary extracted from

  • Takanashi, M.; Shibahara, T.; Shiraki, M.; Saito, T.
    Biochemical and genetic characterization of a D(-)-3-hydroxybutyrate dehydrogenase from Acidovorax sp. strain SA1 (2004), J. Biosci. Bioeng., 97, 78-81.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.30 3-hydroxybutyrate induces the enzyme when contained in the growth medium Acidovorax sp.
1.1.1.30 dithiothreitol
-
 Acidovorax sp.
1.1.1.30 glycerol
-
 Acidovorax sp.
1.1.1.30 Lactate induces the enzyme when contained in the growth medium Acidovorax sp.
1.1.1.30 succinate induces the enzyme when contained in the growth medium Acidovorax sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.30 DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) Acidovorax sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.30 EDTA inhibition and destabilization of the enzyme at 10 mM Acidovorax sp.
1.1.1.30 glucose inhibits the enzyme when contained in the growth medium Acidovorax sp.
1.1.1.30 Hg2+ inhibition at 1 mM, and destabilization at 10 mM Acidovorax sp.
1.1.1.30 Zn2+ inhibition and destabilization of the enzyme at 10 mM Acidovorax sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.30 0.029
-
 NADH reduction reaction, pH 5.0, 55°C Acidovorax sp.
1.1.1.30 0.089
-
 NAD+ oxidation reaction, pH 8.5, 55°C Acidovorax sp.
1.1.1.30 0.24
-
 acetoacetate reduction reaction, pH 5.0, 55°C Acidovorax sp.
1.1.1.30 0.45
-
 (R)-3-hydroxybutyrate oxidation reaction, pH 8.5, 55°C Acidovorax sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.30 Ca2+ stabilizes the enzyme at 10 mM Acidovorax sp.
1.1.1.30 Mg2+ stabilizes the enzyme at 10 mM Acidovorax sp.
1.1.1.30 Mn2+ stabilizes the enzyme at 10 mM Acidovorax sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.30 27000
-
 4 * 27000, SDS-PAGE Acidovorax sp.
1.1.1.30 110000
-
 gel filtration Acidovorax sp.

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-hydroxybutyrate + NAD+ Acidovorax sp. strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB acetoacetate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.30 Acidovorax sp. Q767A0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.30 native by 3 chromatographic steps, recombinant from Escherichia coli in 2chromatographic steps Acidovorax sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.30 72
-
 purified native enzyme Acidovorax sp.
1.1.1.30 300
-
 purified recombinant enzyme Acidovorax sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.30 (R)-3-hydroxybutyrate + NAD+
-
 Acidovorax sp. acetoacetate + NADH + H+
-
 r
1.1.1.30 (R)-3-hydroxybutyrate + NAD+ strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB Acidovorax sp. acetoacetate + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.30 tetramer 4 * 27000, SDS-PAGE Acidovorax sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.30 BDH
-
 Acidovorax sp.
1.1.1.30 D(-)-3-hydroxybutyrate dehydrogenase
-
 Acidovorax sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.30 55
-
-
 Acidovorax sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.30
-
 40
-
 Acidovorax sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.30 4.5 5 reduction reaction Acidovorax sp.
1.1.1.30 8.5
-
 oxidation reaction Acidovorax sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.30 NAD+
-
 Acidovorax sp.
1.1.1.30 NADH
-
 Acidovorax sp.