| 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 | ||||||||
| |||||||||
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
- 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.
| 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 | ||||||||
| |||||||||
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
- 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.