View source for 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

{{Infobox enzyme
| Name = Tyrosine N-monooxygenase
| EC_number = 1.14.13.41
| CAS_number = 159447-19-5
| IUBMB_EC_number = 1/14/13/41
| GO_code = 
| image = 
| width = 
| caption =
}}
'''Tyrosine N-monooxygenase''' ({{EC number|1.14.13.41}}, ''tyrosine N-hydroxylase'', ''CYP79A1'') is an [[enzyme]] with system name ''L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating)''.<ref>{{cite journal | title = The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in <em>Sorghum bicolor</em> (L.) Moench and the involvement of 1-ACI-nitro-2-(<em>p</em>-hydroxyphenyl)ethane as an intermediate |author = Halkier, B.A. and M&oslash;ller, B.L. |journal = J. Biol. Chem. |year = 1990 |volume = 265 |pages = 21114–21121 |pmid = 2250015 |issue=34}}</ref><ref>{{cite journal | title = Cytochrome <em>P</em>-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of <small>L</small>-tyrosine to <em>p</em>-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in <em>Sorghum bicolor</em> (L.) Moench |author = Sibbesen, O., Koch, B., Halkier, B.A. and M&oslash;ller, B.L. |journal = J. Biol. Chem. |year = 1995 |volume = 270 |pages = 3506–3511 |pmid = 7876084 |issue=8}}</ref><ref>{{cite journal | title = Transgenic tobacco and <em>Arabidopsis</em> plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis |author = Bak, S., Olsen, C.E., Halkier, B.A. and Moller, B.L. |journal = Plant Physiol. |year = 2000 |volume = 123 |pages = 1437–1448 |pmid = 10938360 |issue=4 |pmc=59100}}</ref><ref>{{cite journal | title = Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to <em>p</em>-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in <em>Triglochin maritima</em> |author = Nielsen, J.S. and Moller, B.L. |journal = Plant Physiol. |year = 2000 |volume = 122 |pages = 1311–1321 |pmid = 10759528 |doi=10.1104/pp.122.4.1311 |pmc=58967}}</ref><ref>{{cite journal | title = Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants |author = Busk, P.K. and M&oslash;ller, B.L. |journal = Plant Physiol. |year = 2002 |volume = 129 |pages = 1222–1231 |pmid = 12114576 |doi=10.1104/pp.000687 |pmc=166516}}</ref><ref>{{cite journal | title = Metabolic engineering of dhurrin in transgenic <em>Arabidopsis</em> plants with marginal inadvertent effects on the metabolome and transcriptome |author = Kristensen, C., Morant, M., Olsen, C.E., Ekstr&oslash;m, C.T., Galbraith, D.W., M&oslash;ller, B.L. and Bak, S. |journal = Proc. Natl. Acad. Sci. USA |year = 2005 |volume = 102 |pages = 1779–1784 |pmid = 15665094 |doi=10.1073/pnas.0409233102 |pmc=545087}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

:L-[[tyrosine]] + 2 O<sub>2</sub> + 2 NADPH + 2 H<sup>+</sup> <math>\rightleftharpoons</math> (Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP<sup>+</sup> + CO<sub>2</sub> + 3 H<sub>2</sub>O (overall reaction)
:(1a) L-tyrosine + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> N-hydroxy-L-tyrosine + NADP<sup>+</sup> + H<sub>2</sub>O
:(1b) N-hydroxy-L-tyrosine + O<sub>2</sub> + NADPH + H<sup>+</sup> <math>\rightleftharpoons</math> N,N-dihydroxy-L-tyrosine + NADP<sup>+</sup> + H<sub>2</sub>O
:(1c) N,N-dihydroxy-L-tyrosine <math>\rightleftharpoons</math> (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO<sub>2</sub> + H<sub>2</sub>O

Tyrosine N-monooxygenase is [[heme]]-[[thiol]]ate protein (P-450). 

== References ==
{{reflist}}

== External links ==
* {{MeshName|Tyrosine+N-monooxygenase}}

[[Category:EC 1.14.13]]