A7653
L-Alanine Dehydrogenase from Bacillus subtilis
buffered aqueous glycerol solution, ~30 units/mg protein (Lowry)
Sinónimos:
L-Alanine: NAD+ oxidoreductase (deaminating)
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| Tamaño de envase | SKU | Disponibilidad | Precio |
|---|---|---|---|
| 100 units | Comprobar disponibilidad del carrito | MXP 7,009.00 |
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
Specific activity:
~30 units/mg protein (Lowry)
Biological source:
Bacillus subtilis
MXP 7,009.00
Comprobar disponibilidad del carrito
Servicio técnico
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Bacillus subtilis
Quality Level
form
buffered aqueous glycerol solution
specific activity
~30 units/mg protein (Lowry)
foreign activity
LDH ~1% (using pyruvate as substrate)
storage temp.
−20°C
Application
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 [1].
Biochem/physiol Actions
L-Alanine dehydrogenase is an 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.[1] 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.[2]
Physical form
Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7
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.
1 of 1
Este artículo | |||
|---|---|---|---|
| biological source Bacillus subtilis | biological source Bacillus subtilis | biological source - | biological source - |
| specific activity ~30 units/mg protein (Lowry) | specific activity ≥20 units/mg protein (Lowry) | specific activity ≥60 units/mg protein | specific activity ≥4.0 units/mg protein |
| form buffered aqueous glycerol solution | form ammonium sulfate suspension | form lyophilized powder | form aqueous suspension |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C |
| foreign activity LDH ~1% (using pyruvate as substrate) | foreign activity - | foreign activity - | foreign activity - |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 3
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Contenido relacionado
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
Hexigeduleng Bao et al.
Plant, cell & environment, 38(3), 600-613 (2014-07-31)
γ-Aminobutyric acid (GABA) accumulates in many plant species in response to environmental stress. However, the physiological function of GABA or its metabolic pathway (GABA shunt) in plants remains largely unclear. Here, the genes, including glutamate decarboxylases (SlGADs), GABA transaminases (SlGABA-Ts) and
Wei Ye et al.
Microbiological research, 165(4), 268-275 (2009-09-02)
The major objective of the present study is to change the alanine production of Lactic acid bacteria by expression of Bacillus subtilis (natto) alanine dehydrogenase (AlaDH), the gene that is not present in Lactic acid. B. subtilis AlaDH gene (ald)
Número de artículo de comercio global
| SKU | GTIN |
|---|---|
| A7653-100UN | 04061833386026 |