Alanine dehydrogenase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
alanine dehydrogenase
Identifiers
EC number 1.4.1.1
CAS number 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.

his enzyme participates in taurine and hypotaurine metabolism and reductive carboxylate cycle (CO2 fixation).

Nomenclature[edit]

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[edit]

Alanine dehydrogenase contains both a N-terminus[1] and C-terminus domains.[2][3]

References[edit]

  1. ^ Pfam PF05222
  2. ^ Pfam PF01262
  3. ^ 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. 

Further reading[edit]

  • 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. 
  • Yoshida A, Freese E (February 1965). "Enzymic properties of alanine dehydrogenase of Bacillus subtilis". Biochimica et Biophysica Acta. 96: 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.