L-Alanine Dehydrogenase from Bacillus subtilis

Name: <SC>L</SC>-Alanine Dehydrogenase from <I>Bacillus subtilis</I>
Brand: SIGMA

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

Synonym(s):

L-Alanine: NAD⁺ oxidoreductase (deaminating)

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About This Item

CAS Number:

9029-06-5

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

232-847-9

MDL number:

MFCD00131441

EC Number:

1.4.1.1 (BRENDA, IUBMB)

Specific activity:

~30 units/mg protein (Lowry)

Biological source:

Bacillus subtilis

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Properties

biological source

Bacillus subtilis

Quality Segment

200

form

buffered aqueous glycerol solution

specific activity

~30 units/mg protein (Lowry)

foreign activity

LDH ~1% (using pyruvate as substrate)

storage temp.

−20°C

Description

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.