A7653
L-Alanine Dehydrogenase from Bacillus subtilis
buffered aqueous glycerol solution, ~30 units/mg protein (Lowry)
Sinonimo/i:
L-Alanine: NAD+ oxidoreductase (deaminating)
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About This Item
Prodotti consigliati
Origine biologica
Bacillus subtilis
Livello qualitativo
Stato
buffered aqueous glycerol solution
Attività specifica
~30 units/mg protein (Lowry)
Attività estranea
LDH ~1% (using pyruvate as substrate)
Temperatura di conservazione
−20°C
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Applicazioni
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 .
Azioni biochim/fisiol
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. 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.
Definizione di unità
One unit will convert 1.0 μmole of L-alanine to pyruvate and NH3 per min at pH 10.0 at 25 °C.
Stato fisico
Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Dispositivi di protezione individuale
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
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