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Your query returned 1 entry. 
Printable version
| EC | 1.14.14.156 | ||||||||
| Accepted name: | tryptophan N-monooxygenase | ||||||||
| Reaction: | L-tryptophan + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction) (1a) L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O (1b) N-hydroxy-L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O (1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O |
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| Other name(s): | tryptophan N-hydroxylase; CYP79B1; CYP79B2; CYP79B3 | ||||||||
| Systematic name: | L-tryptophan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating) | ||||||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein from the plant Arabidopsis thaliana. This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. | ||||||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
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