ENZYME entry: EC 1.14.14.156
| Accepted Name |
|---|
| Tryptophan N-monooxygenase.
|
| Alternative Name(s) |
|---|
| CYP79B1. |
| CYP79B2. |
| CYP79B3. |
| Tryptophan N-hydroxylase. |
| Reaction catalysed |
|---|
| L-tryptophan + 2 [reduced NADPH--hemoprotein reductase] + 2 O(2) <=> (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O |
| Cofactor(s) |
|---|
| Heme-thiolate.
|
| Comment(s) |
|---|
- A cytochrome P450 (heme-thiolate) protein from the plant Arabidopsis
thaliana.
- This enzyme catalyzes 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
catalyzed by the enzyme.
- Formerly EC 1.14.13.125 and EC 1.14.13.n2.
|
| Cross-references |
|---|
| BRENDA | 1.14.14.156 |
| EC2PDB | 1.14.14.156 |
| ExplorEnz | 1.14.14.156 |
| PRIAM enzyme-specific profiles | 1.14.14.156 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.14.156 |
| IUBMB Enzyme Nomenclature | 1.14.14.156 |
| IntEnz | 1.14.14.156 |
| MEDLINE | Find literature relating to 1.14.14.156 |
| MetaCyc | 1.14.14.156 |
| Rhea expert-curated reactions | 1.14.14.156 |
| UniProtKB/Swiss-Prot |
|
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