EC Number   |
General Information |
Reference |
|---|
   1.14.14.43 | physiological function |
aliphatic oximes derived from chain-elongated homologs of methionine are efficiently metabolized by isoform CYP83A1, whereas CYP83B1 metabolizes these substrates with very low efficiency. Aromatic oximes derived from phenylalanine, tryptophan, and tyrosine are metabolized by both enzymes, although CYP83B1 has higher affinity for these substrates than CYP83A1 |
741196 |
| 1.14.14.43 | physiological function |
ectopic overexpression of CYP83A1 rescues the rnt1-1 phenotype caused by knockout of CYP83B1 and showing a strong auxin excess phenotype |
741195 |
| 1.14.14.43 | physiological function |
ectopic overexpression of isoform CYP83A1.1 in Arabidopsis thaliana. The isoform is involved mainly in the synthesis of C4 aliphatic glucosinolates |
741219 |
| 1.14.14.43 | physiological function |
loss of CYP83A1 function leads to dramatically reduced parasitic growth of the biotrophic powdery mildew fungus Erysiphe cruciferarum on Arabidopsis thaliana. The CYP83A1 mutants support less well the germination and appressorium formation of Erysiphe cruciferarum on the leaf surface and post-penetration conidiophore formation by the fungus. The mutants also lack very-long-chain aldehydes on their leaf surface. When chemically complemented with the C26 aldehyde n-hexacosanal, the mutants can again support appressorium formation. The mutants further accumulate 5-methylthiopentanaldoxime, the potentially toxic substrate of CYP83A1 |
741068 |
