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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
ProductName
EC No.
CAS No.
Source
Price
CatalogNATE-1801
EC No.EC 1.4.1.1
CAS No.9029-06-5
SourceE. coli
CatalogEXWM-1442
EC No.EC 1.4.1.1
CAS No.9029-06-5
Source
CatalogNATE-0044
EC No.EC 1.4.1.1
CAS No.9029-06-5
SourceE. coli
CatalogNATE-0043
EC No.EC 1.4.1.1
CAS No.9029-06-5
SourceBacillus subtil...
Related Services
Related Protocols
L-alanine_dehydrogenase -Enzymatic Assay Protocol
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