Alanine dehydrogenase

In enzymology, an alanine dehydrogenase is an enzyme that catalyzes the chemical reaction


 * L-alanine + H2O + NAD+ $$\rightleftharpoons$$ pyruvate + NH3 + NADH + H+

The 3 substrates of this enzyme are L-alanine, H2O, and NAD+, whereas its 4 products are pyruvate, NH3, NADH, and H+.

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. This enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (co2 fixation).

Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes, , , , , and.