A7189
L-Alanine Dehydrogenase from Bacillus subtilis
ammonium sulfate suspension, ≥20 units/mg protein (Lowry)
别名:
L-Alanine: NAD+ oxidoreductase (deaminating)
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
Specific activity:
≥20 units/mg protein (Lowry)
Biological source:
Bacillus subtilis
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.
存储类别
12 - Non Combustible Liquids
wgk
WGK 2
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis.
Siranosian K, et al.
Journal of Bacteriology, 175(21), 6789-6796 (1993)
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)
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)
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
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
商品
Instructions for working with enzymes supplied as ammonium sulfate suspensions
以硫酸铵悬浮液形式提供的酶的使用指南
全球贸易项目编号
| 货号 | GTIN |
|---|---|
| A7189-250UN | 04061838168511 |
| A7189-500UN | 04061838168528 |
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