Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

View All Documentation

A7189

Sigma-Aldrich

L-Alanine Dehydrogenase from Bacillus subtilis

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

Synonym(s):

L-Alanine: NAD+ oxidoreductase (deaminating)

Sign Into View Organizational & Contract Pricing

Select a Size

250 UNITS
$465.00
500 UNITS
$533.40

$465.00

Available to ship onApril 08, 2025Details

All Photos(1)

Select a Size

Change View
250 UNITS
$465.00
500 UNITS
$533.40

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

$465.00

Available to ship onApril 08, 2025Details

biological source

Bacillus subtilis

Quality Level

200

form

ammonium sulfate suspension

specific activity

≥20 units/mg protein (Lowry)

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

General description

L-Alanine Dehydrogenase has a N-terminal substrate-binding domain and a C-terminal NAD-binding domain.[1]

Application

L-Alanine Dehydrogenase from Bacillus subtilis has been used in the carbon nanotube columns for H2-driven biocatalysis hydrogenation studies.[2]
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 [3].

Biochem/physiol Actions

L-Alanine Dehydrogenase is essential for sporulation in Bacillus subtilis.[4]
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.[3] 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.[5]

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000274150
0000266670
0000262370
099M4116V
11190423

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis.
Siranosian K, et al.
Journal of Bacteriology, 175(21), 6789-6796 (1993)
Domain motions and functionally-key residues of l-alanine dehydrogenase revealed by an elastic network model
Li XY, et al.
International Journal of Molecular Sciences, 16(12), 29383-29397 (2015)
H 2-Driven biocatalytic hydrogenation in continuous flow using enzyme-modified carbon nanotube columns
Zor C, et al.
Chemical Communications (Cambridge, England), 53(71), 9839-9841 (2017)
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
Nadine Bongaerts et al.
Nature communications, 13(1), 3905-3905 (2022-07-08)
Whole-cell screening for Mycobacterium tuberculosis (Mtb) inhibitors is complicated by the pathogen's slow growth and biocontainment requirements. Here we present a synthetic biology framework for assaying Mtb drug targets in engineered E. coli. We construct Target Essential Surrogate E. coli
View All Related Papers

Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Questions

Reviews

No rating value

Active Filters

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service