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.
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.
CYP79B2 is not inhibited by Me2SO of a maximum concentration of 4% (v/v); the combination of 100 mM H2O2, 1 mM MnCl2, and 800 mM 2,4-dichlorophenol added to the reconstitution assay inhibits the CYP79B2 activity by 99%
cyp79B2/cyp79B3 double mutant has reduced levels of indole-3-acetic acid, shows growth defects consistent with partial auxin deficiency, and is hypersensitive to 5-methyltryptophan
depletion of tryptophan-derived metabolites in cyp79B2/cyp79B3 mutants renders Arabidopsis fully susceptible to non-adapted Plectosphaerella cucumerina isolates 1187 and 2127, and super-susceptible to the adapted Plectosphaerella cucumerina isolate BMM
CYP79B2, when overexpressed in Arabidopsis, confers resistance to toxic analogs of L-tryptophan like 5-methyltryptophan, 5-methylanthranilate, 5-fluoroindole, and 5-fluorotryptophan. In addition, CYP79B2 is expressed in response to bacterial pathogens. CYP79B2 metabolizes L-tryptophan to indole-3-acetaldoxime that can be used for either indole-3-acetic acid or indole glucosinolate biosynthesis; CYP79B3 metabolize L-tryptophan to indole-3-acetaldoxime that can be used for either indole-3-acetic acid or indole glucosinolate biosynthesis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP79B2 expression is induced up to 1.5fold by wounding, 2.8fold by 0.25 mM methyl jasmonate in combination with 2.5 mM 1-aminocyclopropane-1-carboxylate, and 4.6fold after methyl jasmonate treatment alone. CYP79B3 is induced 3.5fold by methyl jasmonate and up to 1.7fold by methyl jasmonate in combination with 1-aminocyclopropane-1-carboxylate, and the induction levels are lower than those observed for CYP79B2. After treatment with 0.0002 mM 2,4-dichloro-phenoxyacetic acid, expression of CYP79B2 and CYP79B3 is induced 1.6 and 1.3fold, respectively
Mikkelsen, M.; Hansen, C.; Wittstock, U.; Halkier, B.
Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid
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1.14.14.156 tryptophan N-monooxygenase
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