Alanine dehydrogenase

Alanine dehydrogenase () is an enzyme that catalyzes the chemical reaction
The 2 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+ because water is 55M and does not change, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion.
This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle ( fixation).
Nomenclature.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. T
Structure.
Alanine dehydrogenase contains both a N-terminus and C-terminus domains.