Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

L-tyrosine,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)

L-tyrosine + 2 O2 + 2 [reduced NADPH---hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH---hemoprotein reductase] + CO2 + 3 H2O (overall reaction) [RN:R10671];
(1a) L-tyrosine + O2 + [reduced NADPH---hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R00730];
(1b) N-hydroxy-L-tyrosine + O2 + [reduced NADPH---hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R04460];
(1c) N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O [RN:R07190]

R00730 R04460 R07190 R10671

L-tyrosine [CPD:C00082];
O2 [CPD:C00007];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
N-hydroxy-L-tyrosine [CPD:C03004];
N,N-dihydroxy-L-tyrosine [CPD:C15503]

A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum, along with EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase and EC 2.4.1.85, cyanohydrin beta-glucosyltransferase. Some 2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product.

EC 1.14.14.36 created 1992 as EC 1.14.13.41, modified 2001, modified 2005, transferred 2016 to EC 1.14.14.36

1  [PMID:2250015]

Halkier BA, Moller BL.

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 (1990) 21114-21.

2  [PMID:7876084]

Sibbesen O, Koch B, Halkier BA, Moller BL.

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 (1995) 3506-11.

3  [PMID:10049494]

Kahn RA, Fahrendorf T, Halkier BA, Moller BL.

Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.

Arch. Biochem. Biophys. 363 (1999) 9-18.

4  [PMID:10938360]

Bak S, Olsen CE, Halkier BA, Moller BL.

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 (2000) 1437-48.

5  [PMID:10759528]

Nielsen JS, Moller BL.

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 (2000) 1311-21.

[ag:AAF66543 AAF66544]

6  [PMID:12114576]

Busk PK, Moller BL.

Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants.

Plant. Physiol. 129 (2002) 1222-31.

7  [PMID:15665094]

Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller BL, Bak S.

Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome.

Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1779-84.

8  [PMID:26361733]

Clausen M, Kannangara RM, Olsen CE, Blomstedt CK, Gleadow RM, Jorgensen K, Bak S, Motawie MS, Moller BL

The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.

Plant. J. 84 (2015) 558-73.