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A7653

Sigma-Aldrich

L-Alanine Dehydrogenase from Bacillus subtilis

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

Synonym(s):

L-Alanine: NAD+ oxidoreductase (deaminating)

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100 UNITS
$317.30

$317.30

List price$334.00
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100 UNITS
$317.30

About This Item

CAS Number:
9029-06-5
EC Number:
1.4.1.1 (BRENDA, IUBMB)
EC Number:
232-847-9
MDL number:
MFCD00131441
UNSPSC Code:
12352204
NACRES:
NA.54

$317.30

List price$334.00
Web-Only Promotion

Available to ship onApril 08, 2025Details

biological source

Bacillus subtilis

Quality Level

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

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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]

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

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

ppe

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

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Certificates of Analysis (COA)

Lot/Batch Number
0000380060
0000279721
0000380060
0000279721
11181151

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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
Wei Ye et al.
Microbiological research, 165(4), 268-275 (2009-09-02)
The major objective of the present study is to change the alanine production of Lactic acid bacteria by expression of Bacillus subtilis (natto) alanine dehydrogenase (AlaDH), the gene that is not present in Lactic acid. B. subtilis AlaDH gene (ald)
Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations.
Sarvind Mani Tripathi et al.
Proteins, 72(3), 1089-1095 (2008-05-21)
Karin Denger et al.
Microbiology (Reading, England), 152(Pt 11), 3197-3206 (2006-11-01)
A degradative pathway for taurine (2-aminoethanesulfonate) in Rhodobacter sphaeroides 2.4.1 was proposed by Brüggemann et al. (2004) (Microbiology 150, 805-816) on the basis of a partial genome sequence. In the present study, R. sphaeroides 2.4.1 was found to grow exponentially
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