Description
L-Alanine dehydrogenase is a stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the generation of pyruvate during sporulation.
Abbr
AlaDH, Native (Bacillus stearothermophilus)
Source
Bacillus stearothermophilus
Applications
The enzyme is useful for determination of L-alanine.
Enzyme Commission Number
EC 1.4.1.1
Contaminants
(as AlaDH activity = 100 %)
NADH oxidase: <0.01 %;
Lactate dehydrogenase: <0.10 %.
Molecular Weight
ca. 230,000; Subunit molecular weight : ca. 38,000.
Michaelis Constant
(125 mM Glycine-NaOH buffer, pH 10.5, at 30 °C)
L-Alanine: 10.0 mM;
NAD+: 0.26 mM.
Specificity
L-Alanine: 100 %;
L-Leucine: 0 %;
L-Isoleucine: 0 %.
Unit Definition
One unit of activity is defined as the amount of AlaDH that forms 1 μmol of NADH per minute at 30 °C.
Thermal stability
No detectable decrease in activity up to 70 °C.
Storage
Stable at -20 °C for at least one year.
Synonyms
L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase
Specific Activity
more than 55 U/mg protein
Reaction
L-Alanine + NAD+ + H2O ←→ Pyruvate + NH4+ + NADH
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