Tryptophan dehydrogenase

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tryptophan dehydrogenase
Identifiers
EC no. 1.4.1.19
CAS no. 94047-13-9
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
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PMC articles
PubMed articles
NCBI proteins

In enzymology, tryptophan dehydrogenase (EC 1.4.1.19) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
Tryptophan dehydrogenase
H2O
H+
 
+ NADH + NH3
 

The three substrates of this enzyme are L-tryptophan, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are indole-3-pyruvic acid, ammonia, reduced NADH, and a proton. Nicotinamide adenine dinucleotide phosphate can be used as an alternative cofactor. [1] [2]

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-tryptophan:NAD(P)+ oxidoreductase (deaminating). Other names in common use include NAD(P)+-L-tryptophan dehydrogenase, L-tryptophan dehydrogenase, L-Trp-dehydrogenase, and TDH. This enzyme has at least one effector, calcium.

References

  1. Enzyme 1.4.1.19 at KEGG Pathway Database.
  2. Vacková, Květa; Mehta, Archana; Kutáček, M. (1985). "Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves: The effect of calcium ions on tryptophan dehydrogenase". Biologia Plantarum. 27 (2–3): 154–158. doi:10.1007/BF02902153.