The Enzyme Database

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EC 1.14.14.36     
Accepted name: tyrosine N-monooxygenase
Reaction: L-tyrosine + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
For diagram of dhurrin biosynthesis, click here
Other name(s): tyrosine N-hydroxylase; CYP79A1
Systematic name: L-tyrosine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 159447-19-5
References:
1.  Halkier, B.A. and Møller, B.L. 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) 21114–21121. [PMID: 2250015]
2.  Sibbesen, O., Koch, B., Halkier, B.A. and Møller, B.L. 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) 3506–3511. [PMID: 7876084]
3.  Bennett, R.N., Kiddle, G. and Wallsgrove, R.M. Involvement of cytochrome P450 in glucosinolate biosynthesis in white mustard (a biochemical anomaly). Plant Physiol. 114 (1997) 1283–1291. [PMID: 12223771]
4.  Kahn, R.A., Fahrendorf, T., Halkier, B.A. and Møller, B.L. 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. [PMID: 10049494]
5.  Bak, S., Olsen, C.E., Halkier, B.A. and Møller, B.L. 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) 1437–1448. [PMID: 10938360]
6.  Nielsen, J.S. and Møller, B.L. 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) 1311–1321. [PMID: 10759528]
7.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [PMID: 12114576]
8.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [PMID: 15665094]
9.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [PMID: 26361733]
[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]
 
 


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