| 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).
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Transamination reaction mechanism
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Cori Cycle
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Conversion of Pyruvate into Acetyl-CoA (PDC)
Transcription
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.
This page was last edited on 26 August 2023, at 13:01