Direkt zum Inhalt
Merck

A7653

L-Alanin-Dehydrogenase aus Bacillus subtilis

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

Synonym(e):

L-Alanin: NAD+ -Oxidoreduktase

Anmelden zur Ansicht der Organisations- und Vertragspreise.

Größe auswählen

100 UNITS

€ 302,00

€ 302,00


Warenkorb auf Verfügbarkeit prüfen


Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-847-9
MDL number:
EG-Nummer:
Specific activity:
~30 units/mg protein (Lowry)
Biological source:
Bacillus subtilis

Fortfahren mit

Technischer Dienst
Benötigen Sie Hilfe? Unser Team von erfahrenen Wissenschaftlern ist für Sie da.
Unterstützung erhalten

biological source

Bacillus subtilis

Quality Level

form

buffered aqueous glycerol solution

specific activity

~30 units/mg protein (Lowry)

foreign activity

LDH ~1% (using pyruvate as substrate)

storage temp.

−20°C

Suchen Sie nach ähnlichen Produkten? Aufrufen Leitfaden zum Produktvergleich

Ähnliche Artikel vergleichen

Vollständigen Vergleich anzeigen

Unterschiede anzeigen

1 of 4

Dieser Artikel
A7189L5135A9378
specific activity

~30 units/mg protein (Lowry)

specific activity

≥20 units/mg protein (Lowry)

specific activity

≥60 units/mg protein

specific activity

≥4.0 units/mg protein

biological source

Bacillus subtilis

biological source

Bacillus subtilis

biological source

-

biological source

-

form

buffered aqueous glycerol solution

form

ammonium sulfate suspension

form

lyophilized powder

form

aqueous suspension

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

foreign activity

LDH ~1% (using pyruvate as substrate)

foreign activity

-

foreign activity

-

foreign activity

-

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 [1].

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.[1] 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.[2]

Physical form

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

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Lagerklasse

10 - Combustible liquids

wgk

WGK 3

ppe

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


Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number

Die passende Version wird nicht angezeigt?

Wenn Sie eine bestimmte Version benötigen, können Sie anhand der Lot- oder Chargennummer nach einem spezifischen Zertifikat suchen.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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
A Sinem Ozyurt et al.
Proteins, 72(1), 184-196 (2008-01-25)
This study describes a method to computationally assess the function of homologous enzymes through small molecule binding interaction energy. Three experimentally determined X-ray structures and four enzyme models from ornithine cyclo-deaminase, alanine dehydrogenase, and mu-crystallin were used in combination with
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

Global Trade Item Number

SKUGTIN
A7653-100UN04061833386026

Questions

Reviews

No rating value

Active Filters

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung