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Merck

A7653

Sigma-Aldrich

L-Alanin-Dehydrogenase aus Bacillus subtilis

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

Synonym(e):

L-Alanin: NAD+ -Oxidoreduktase

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

Bacillus subtilis

Qualitätsniveau

Form

buffered aqueous glycerol solution

Spezifische Aktivität

~30 units/mg protein (Lowry)

Fremdaktivität

LDH ~1% (using pyruvate as substrate)

Lagertemp.

−20°C

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Anwendung

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. Wirkung

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.

Einheitendefinition

One unit will convert 1.0 μmole of L-alanine to pyruvate and NH3 per min at pH 10.0 at 25 °C.

Physikalische Form

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

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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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
Hexigeduleng Bao et al.
Plant, cell & environment, 38(3), 600-613 (2014-07-31)
γ-Aminobutyric acid (GABA) accumulates in many plant species in response to environmental stress. However, the physiological function of GABA or its metabolic pathway (GABA shunt) in plants remains largely unclear. Here, the genes, including glutamate decarboxylases (SlGADs), GABA transaminases (SlGABA-Ts) and
Xueli Zhang et al.
Applied microbiology and biotechnology, 77(2), 355-366 (2007-09-18)
Escherichia coli W was genetically engineered to produce L: -alanine as the primary fermentation product from sugars by replacing the native D: -lactate dehydrogenase of E. coli SZ194 with alanine dehydrogenase from Geobacillus stearothermophilus. As a result, the heterologous alanine
Toru Jojima et al.
Applied microbiology and biotechnology, 87(1), 159-165 (2010-03-11)
Corynebacterium glutamicum was genetically engineered to produce L-alanine from sugar under oxygen deprivation. The genes associated with production of organic acids in C. glutamicum were inactivated and the alanine dehydrogenase gene (alaD) from Lysinibacillus sphaericus was overexpressed to direct carbon
Senay Hamarat Baysal et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 35(4), 391-403 (2007-08-19)
Urease and AlaDH enzymes immobilized on active PEG derivatives were encapsulated at different ratios within sheep erythrocytes and their activity, encapsulation yields and erythrocyte recovery levels were assessed. Encapsulated derivatives were administered at given dosages and at given intervals to

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