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Tryptophan dehydrogenase

From Wikipedia, the free encyclopedia
tryptophan dehydrogenase
Identifiers
EC no.1.4.1.19
CAS no.94047-13-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

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

L-tryptophan + NAD(P)+ + H2O (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+

The 4 substrates of this enzyme are L-tryptophan, NAD+, NADP+, and H2O, whereas its 5 products are (indol-3-yl)pyruvate, NH3, NADH, NADPH, and H+.

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

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  • Vackova K, Mehta A, Kutacek M (1985). "Tryptophan aminotransferase and tryptophan dehydrogenase - activities in some cell compartments of spinach leaves - the effect of calcium-ions on tryptophan dehydrogenase". Biol. Plant. 27 (2–3): 154–158. doi:10.1007/BF02902153.