73063
Alanine Dehydrogenase, recombinant
recombinant, expressed in E. coli, ≥15 U/mg
recombinant
expressed in E. coli
Quality Level
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 .
Other Notes
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).
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Regulatory Information
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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
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
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
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
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.
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