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:
Product Name
L-Alanine Dehydrogenase from Bacillus subtilis, ammonium sulfate suspension, ≥20 units/mg protein (Lowry)
biological source
Bacillus subtilis
form
ammonium sulfate suspension
specific activity
≥20 units/mg protein (Lowry)
storage temp.
2-8°C
Quality Level
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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.
General description
L-Alanine Dehydrogenase has a N-terminal substrate-binding domain and a C-terminal NAD-binding domain.
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.
Physical form
Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
Domain motions and functionally-key residues of l-alanine dehydrogenase revealed by an elastic network model
Li XY, et al.
International Journal of Molecular Sciences, 16(12), 29383-29397 (2015)
Dariel Márquez et al.
Frontiers in microbiology, 12, 695382-695382 (2021-08-24)
The γ-aminobutyric acid (GABA) shunt constitutes a conserved metabolic route generating nicotinamide adenine dinucleotide phosphate (NADPH) and regulating stress response in most organisms. Here we show that in the presence of GABA, Saccharomyces cerevisiae produces glutamate and alanine through the
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