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Enzymes for Research, Diagnostic and Industrial Use

AlaDH

Official Full Name
AlaDH
Background
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. 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.
Synonyms
L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase
Catalog Product Name EC No. CAS No. Source Price
NATE-1899 Native Bacillus stearothermophilus Alanine Dehydrogenase EC 1.4.1.1 9029-06-5 Bacillus stearo... Inquiry
NATE-1801 Alanine Dehydrogenase (Crude Enzyme) EC 1.4.1.1 9029-06-5 E. coli Inquiry
EXWM-1442 alanine dehydrogenase EC 1.4.1.1 9029-06-5 Inquiry
NATE-0044 Alanine Dehydrogenase from Bacillus cereus, Recombinant EC 1.4.1.1 9029-06-5 E. coli Inquiry
NATE-0043 Native Bacillus subtilis L-Alanine Dehydrogenase EC 1.4.1.1 9029-06-5 Bacillus subtil... Inquiry
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