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Literature summary for 1.1.1.30 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
Search for more literature for 1.1.1.30

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Acidovorax sp. Q767A0
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Acidovorax sp.
NADH
-
 Acidovorax sp.