Alanine dehydrogenase
| alanine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.1 | ||||||||
| CAS no. | 9029-06-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction
- L-alanine + H2O + NAD+ pyruvate + NH3 + NADH + H+
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 (CO2 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[1] and C-terminus domains.[2][3]
References
- ^ Pfam PF05222
- ^ Pfam PF01262
- ^ Tripathi SM, Ramachandran R (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. 72 (3): 1089–95. doi:10.1002/prot.22101. PMID 18491387. S2CID 23999004.
Further reading
- O'Connor RJ, Halvorson H (March 1961). "The substrate specificity of L-alanine dehydrogenase". Biochimica et Biophysica Acta. 48 (1): 47–55. doi:10.1016/0006-3002(61)90513-3. PMID 13730044.
- Pierard A; Wiame JM (1960). "Proprietes de la L(+)-alanine-deshydrogenase". Biochim. Biophys. Acta. 37 (3): 490–502. doi:10.1016/0006-3002(60)90506-0. PMID 14432812.
- Yoshida A, Freese E (February 1965). "Enzymic properties of alanine dehydrogenase of Bacillus subtilis". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 96 (2): 248–62. doi:10.1016/0926-6593(65)90009-3. PMID 14298830.
- Tripathi SM, Ramachandran R (August 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. 72 (3): 1089–95. doi:10.1002/prot.22101. PMID 18491387. S2CID 23999004.
