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A7189

L-Alanin-Dehydrogenase aus Bacillus subtilis

ammonium sulfate suspension, ≥20 units/mg protein (Lowry)

Synonym(e):

L-Alanin: NAD+ -Oxidoreduktase

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Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
EG-Nummer:
Specific activity:
≥20 units/mg protein (Lowry)
Biological source:
Bacillus subtilis
Technischer Dienst
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Unterstützung erhalten


biological source

Bacillus subtilis

Quality Segment

form

ammonium sulfate suspension

specific activity

≥20 units/mg protein (Lowry)

storage temp.

2-8°C

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.


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