EC Number |
Title |
Organism |
---|
1.14.14.36 | Application of nanodisc technology for direct electrochemical investigation of plant cytochrome P450s and their NADPH P450 oxidoreductase |
Sorghum bicolor |
1.14.14.36 | Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima |
Triglochin maritima |
1.14.14.36 | Conn, E.E.: The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor |
Sorghum bicolor |
1.14.14.36 | Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench |
Sorghum bicolor |
1.14.14.36 | Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants |
Sorghum bicolor |
1.14.14.36 | Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum |
Sorghum bicolor |
1.14.14.36 | Isolation of the heme-thiolate enzyme chytochrome P-450tyr, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench |
Sorghum bicolor |
1.14.14.36 | Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome |
Sorghum bicolor |
1.14.14.36 | Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli |
Sorghum bicolor |
1.14.14.36 | Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench |
Sorghum bicolor |