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| 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 systematic name L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
L-tyrosine + 2 O2 + 2 NADPH + 2 H+(Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-tyrosine + O2 + NADPH + H+
(1b) N-hydroxy-L-tyrosine + O2 + NADPH + H+
(1c) N,N-dihydroxy-L-tyrosine
Tyrosine N-monooxygenase is heme-thiolate protein (P-450).
References
1. ^{{cite journal | vauthors = Halkier BA, Møller BL | title = 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 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 34 | pages = 21114–21 | date = December 1990 | pmid = 2250015 }}
2. ^{{cite journal | vauthors = Sibbesen O, Koch B, Halkier BA, Møller BL | title = 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 | journal = The Journal of Biological Chemistry | volume = 270 | issue = 8 | pages = 3506–11 | date = February 1995 | pmid = 7876084 | doi = 10.1074/jbc.270.8.3506 }}
3. ^{{cite journal | vauthors = Bak S, Olsen CE, Halkier BA, Møller BL | title = 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 | journal = Plant Physiology | volume = 123 | issue = 4 | pages = 1437–48 | date = August 2000 | pmid = 10938360 | pmc = 59100 | doi = 10.1104/pp.123.4.1437 }}
4. ^{{cite journal | vauthors = Nielsen JS, Møller BL | title = Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima | journal = Plant Physiology | volume = 122 | issue = 4 | pages = 1311–21 | date = April 2000 | pmid = 10759528 | pmc = 58967 | doi = 10.1104/pp.122.4.1311 }}
5. ^{{cite journal | vauthors = Busk PK, Møller BL | title = Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants | journal = Plant Physiology | volume = 129 | issue = 3 | pages = 1222–31 | date = July 2002 | pmid = 12114576 | pmc = 166516 | doi = 10.1104/pp.000687 }}
6. ^{{cite journal | vauthors = Kristensen C, Morant M, Olsen CE, Ekstrøm CT, Galbraith DW, Møller BL, Bak S | title = Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 5 | pages = 1779–84 | date = February 2005 | pmid = 15665094 | pmc = 545087 | doi = 10.1073/pnas.0409233102 }}
2. ^{{cite journal | vauthors = Sibbesen O, Koch B, Halkier BA, Møller BL | title = 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 | journal = The Journal of Biological Chemistry | volume = 270 | issue = 8 | pages = 3506–11 | date = February 1995 | pmid = 7876084 | doi = 10.1074/jbc.270.8.3506 }}
3. ^{{cite journal | vauthors = Bak S, Olsen CE, Halkier BA, Møller BL | title = 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 | journal = Plant Physiology | volume = 123 | issue = 4 | pages = 1437–48 | date = August 2000 | pmid = 10938360 | pmc = 59100 | doi = 10.1104/pp.123.4.1437 }}
4. ^{{cite journal | vauthors = Nielsen JS, Møller BL | title = Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima | journal = Plant Physiology | volume = 122 | issue = 4 | pages = 1311–21 | date = April 2000 | pmid = 10759528 | pmc = 58967 | doi = 10.1104/pp.122.4.1311 }}
5. ^{{cite journal | vauthors = Busk PK, Møller BL | title = Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants | journal = Plant Physiology | volume = 129 | issue = 3 | pages = 1222–31 | date = July 2002 | pmid = 12114576 | pmc = 166516 | doi = 10.1104/pp.000687 }}
6. ^{{cite journal | vauthors = Kristensen C, Morant M, Olsen CE, Ekstrøm CT, Galbraith DW, Møller BL, Bak S | title = Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 5 | pages = 1779–84 | date = February 2005 | pmid = 15665094 | pmc = 545087 | doi = 10.1073/pnas.0409233102 }}
External links
- {{MeshName|Tyrosine+N-monooxygenase}}
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