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Alanine dehydrogenase
| Field | Value |
|---|---|
| Name | alanine dehydrogenase |
| EC_number | 1.4.1.1 |
| CAS_number | 9029-06-5 |
| GO_code | 0000286 |
Alanine dehydrogenase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are alanine, water, and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are pyruvic acid, reduced NADH, ammonia, and a proton.
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.
References
References
- {{KEGG enzyme. 1.4.1.1
- (March 1961). "The substrate specificity of L-alanine dehydrogenase". Biochimica et Biophysica Acta.
- (February 1965). "Enzymic properties of alanine dehydrogenase of Bacillus subtilis". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation.
- {{Pfam. PF05222
- {{Pfam. PF01262
- (2008). "Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures "open" and "closed" enzyme conformations". Proteins.
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