Alanine dehydrogenase

In enzymology, an alanine dehydrogenase (EC number|1.4.1.1) is an enzyme that catalyzes the chemical reaction

:L-alanine + H₂O + NAD⁺ $ightleftharpoons$ 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).

tructural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1OMO, PDB link|1PJB, PDB link|1PJC, PDB link|1SAY, PDB link|1VLL, and PDB link|2EEZ.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|9029-06-5."

Gene Ontology (GO) codes