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A7653 Sigma

L-Alanine Dehydrogenase from Bacillus subtilis

buffered aqueous glycerol solution, ~30 units/mg protein (Lowry)

Synonym: L-Alanine: NAD+ oxidoreductase (deaminating)

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Properties

Related Categories 1.4.x.x Acting on CH-NH2, 1.x.x.x Oxidoreductases, Amino Acid Metabolism, Biochemicals and Reagents, Cell Biology,
form   buffered aqueous glycerol solution
foreign activity   LDH ~1% (using pyruvate as substrate)
storage temp.   −20°C

Description

Packaging

100 units in glass bottle

Unit Definition

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

Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7

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 .

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. 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.

Price and Availability


All labs need water
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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