A7189
L-Alanine Dehydrogenase from Bacillus subtilis
ammonium sulfate suspension, ≥20 units/mg protein (Lowry)
Synonym(s):
L-Alanine: NAD+ oxidoreductase (deaminating)
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
Specific activity:
≥20 units/mg protein (Lowry)
Biological source:
Bacillus subtilis
biological source
Bacillus subtilis
Quality Level
form
ammonium sulfate suspension
specific activity
≥20 units/mg protein (Lowry)
storage temp.
2-8°C
General description
L-Alanine Dehydrogenase has a N-terminal substrate-binding domain and a C-terminal NAD-binding domain.
Application
L-Alanine Dehydrogenase from Bacillus subtilis has been used in the carbon nanotube columns for H2-driven biocatalysis hydrogenation studies.
L-Alanine dehydrogenase converts L-alanine to pyruvate and ammonium. L-Alanine dehydrogenase from Bacillus subtilis may be used to study enzyme inactivation and protection .
Biochem/physiol Actions
L-Alanine Dehydrogenase is essential for sporulation in Bacillus subtilis.
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. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L- or D-cysteine.
Physical form
Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0
Other Notes
One unit will convert 1.0 μmole of L-alanine to pyruvate and NH3 per min at pH 10.0 at 25 °C.
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Storage Class
12 - Non Combustible Liquids
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Related Content
H 2-Driven biocatalytic hydrogenation in continuous flow using enzyme-modified carbon nanotube columns
Zor C, et al.
Chemical Communications (Cambridge, England), 53(71), 9839-9841 (2017)
Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis.
Siranosian K, et al.
Journal of Bacteriology, 175(21), 6789-6796 (1993)
D Delforge et al.
The Journal of biological chemistry, 272(4), 2276-2284 (1997-01-24)
L-Alanine dehydrogenase from Bacillus subtilis was inactivated with two different lysine-directed chemical reagents, i.e. 2,4, 6-trinitrobenzenesulfonic acid and N-succinimidyl 3-(2-pyridyldithio)propionate. In both cases, the inactivation followed pseudo first-order kinetics, with a 1:1 stoichiometric ratio between the reagent and the enzyme