EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
1.14.14.36 | 660383 |
Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome |
Proc. Natl. Acad. Sci. USA |
102 |
1779-1784 |
2005 |
Sorghum bicolor |
15665094 |
1.14.14.36 | 739339 |
Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum |
Plant Physiol. |
115 |
1661-1670 |
1997 |
Sorghum bicolor |
9414567 |
1.14.14.36 | 739340 |
Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima |
Plant Physiol. |
122 |
1311-1321 |
2000 |
Triglochin maritima |
10759528 |
1.14.14.36 | 739341 |
Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis |
Plant Physiol. |
123 |
1437-1448 |
2000 |
Sorghum bicolor |
10938360 |
1.14.14.36 | 660217 |
Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants |
Plant Physiol. |
129 |
1222-1231 |
2002 |
Sorghum bicolor |
12114576 |
1.14.14.36 | 285331 |
Conn, E.E.: The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor |
J. Biol. Chem. |
250 |
4708-4713 |
1975 |
Sorghum bicolor |
237909 |
1.14.14.36 | 348459 |
The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate |
J. Biol. Chem. |
265 |
21114-21121 |
1990 |
Sorghum bicolor |
2250015 |
1.14.14.36 | 738563 |
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 |
J. Biol. Chem. |
270 |
3506-3511 |
1995 |
Sorghum bicolor |
7876084 |
1.14.14.36 | 390080 |
Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli |
Arch. Biochem. Biophys. |
322 |
369-377 |
1995 |
Sorghum bicolor |
7574710 |
1.14.14.36 | 390079 |
The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench |
Arch. Biochem. Biophys. |
323 |
177-186 |
1995 |
Sorghum bicolor |
7487064 |