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73063

Sigma-Aldrich

Alanine Dehydrogenase, recombinant

recombinant, expressed in E. coli, ≥15 U/mg

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

crystals
powder

specific activity

≥15 U/mg

storage temp.

−20°C

Application

Alanine dehydrogenase (ald) is an oxidoreductase that is involved in taurin/hypotaurine metabolism and CO2 fixation. It is used in various enzyme assays and in kinetic studies .

Biochem/physiol Actions

Alanine dehydrogenase catalyzes the reversible reductive amination of pyruvate using NADH as an oxidation/reduction cofactor .

Unit Definition

1 U corresponds to the amount of enzyme which converts 1 μmol L-alanine per minute at pH 10.0 and 30°C (NAD as cofactor).

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


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M T Smith et al.
The Journal of biological chemistry, 268(15), 10746-10753 (1993-05-25)
The kinetic mechanism of alanine dehydrogenase from soybean nodule bacteroids was studied by initial velocity experiments with or without product inhibitors, dead-end inhibitors, or alternate substrates. Without inhibitors, double-reciprocal plots of initial velocity experiments showed intersecting lines, indicating a sequential
Roxane Lahmi et al.
Journal of bacteriology, 188(14), 5258-5265 (2006-07-04)
Degradation of the cyanobacterial light-harvesting antenna, the phycobilisome, is a general acclimation response that is observed under various stress conditions. In this study we identified a novel mutant of Synechococcus elongatus PCC 7942 that exhibits impaired phycobilisome degradation specifically during
Sivagamisundaram Chavadi et al.
Journal of bacteriology, 191(24), 7545-7553 (2009-10-13)
To better understand the global effects of "natural" lesions in genes involved in the pyruvate metabolism in Mycobacterium bovis, null mutations were made in the Mycobacterium tuberculosis H37Rv ald and pykA genes to mimic the M. bovis situation. Like M.
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
Daniel Agren et al.
Journal of molecular biology, 377(4), 1161-1173 (2008-02-29)
L-alanine dehydrogenase from Mycobacterium tuberculosis catalyzes the NADH-dependent reversible conversion of pyruvate and ammonia to L-alanine. Expression of the gene coding for this enzyme is up-regulated in the persistent phase of the organism, and alanine dehydrogenase is therefore a potential

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