L-ALANINE DEHYDROGENASE FROM BACILLUS SUBTILIS AMMONIUM SULFATE SUSPENSION >=20 UNITS/MG PROTEIN (LOWRY) (C005B-002529)

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.

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

Suspension in 2.4 M (NH₄)₂SO₄ solution, pH 7.0

biological source: Bacillus subtilis. Quality Level: 200. form: ammonium sulfate suspension. specific activity: ≥. 20 . units/mg protein (Lowry). storage temp.: 2-8°C. Storage Class Code: 12 - Non Combustible Liquids. WGK: WGK 2. Flash Point(F): Not applicable. Flash Point(C): Not applicable. Personal Protective Equipment: Eyeshields, Gloves, multi-purpose combination respirator cartridge (US).