1.14.14.36	physiological function	a microsomal fraction from seedlings of Sorghum bicolor catalyzes the conversion of L-tyrosine to 4-hydroxymandelonitrile via 4-hydroxyphenylacetaldoxime	285331	
1.14.14.36	physiological function	at all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes. During development, the activity of tyrosine N-monooxygenase CYP79A1 is lower than the activity of 4-hydroxyphenylacetaldehyde oxime monooxygenase CYP71E1, suggesting that CYP79A1 catalyzes the rate-limiting step in dhurrin synthesis	660217	
1.14.14.36	physiological function	full length CYP79A1, CYP71E1 and NADPH P450 oxidoreductase of the dhurrin pathway are reconstituted individually in nanoscale lipid patches, nanodiscs, and directly immobilized on unmodified gold electrodes. Cyclic voltammograms of CYP79A1 and CYP71E1 reveal reversible redox peaks with average midpoint potentials of 80 mV and 72 mV vs. Ag/AgCl, respectively. NADPH P450 oxidoreductase yields two pairs of redox peaks with midpoint potentials of 90 mV and -300 mV, respectively. The average heterogeneous electron transfer rate constant is calculated to be 1.5 per s	739696	
1.14.14.36	physiological function	multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima	739340	
1.14.14.36	physiological function	multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima. When CYP79E1 is reconstituted with CYP71E1 and NADPH-cytochrome P450 oxidoreductase from Sorghum bicolor, efficient conversion of tyrosine to p-hydroxymandelonitrile is observed	739340	
1.14.14.36	physiological function	the biosynthetic pathway for the cyanogenic glucoside dhurrin in Sorghum involves the sequential production of (E)- and (Z)-4-hydroxyphenylacetaldoxime. Monooxygenae CYP79A1 catalyzes conversion of tyrosine to (E)-4-hydroxyphenylacetaldoxime, whereas monooxygenase CYP71E1 catalyzes conversion of (E)-4-hydroxyphenylacetaldoxime into the corresponding geometrical Z-isomer as required for its dehydration into a nitrile, the next intermediate in cyanogenic glucoside synthesis	739318