Biology:Tyrosine N-monooxygenase
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Short description: Class of enzymes
| Tyrosine N-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.41 | ||||||||
| CAS number | 159447-19-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Tyrosine N-monooxygenase (EC 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+ [math]\displaystyle{ \rightleftharpoons }[/math] (Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP+ + CO2 + 3 H2O (overall reaction)
- (1a) L-tyrosine + O2 + NADPH + H+ [math]\displaystyle{ \rightleftharpoons }[/math] N-hydroxy-L-tyrosine + NADP+ + H2O
- (1b) N-hydroxy-L-tyrosine + O2 + NADPH + H+ [math]\displaystyle{ \rightleftharpoons }[/math] N,N-dihydroxy-L-tyrosine + NADP+ + H2O
- (1c) N,N-dihydroxy-L-tyrosine [math]\displaystyle{ \rightleftharpoons }[/math] (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
Tyrosine N-monooxygenase is heme-thiolate protein (P-450).
References
- ↑ "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". The Journal of Biological Chemistry 265 (34): 21114–21. December 1990. doi:10.1016/S0021-9258(17)45334-8. PMID 2250015.
- ↑ "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". The Journal of Biological Chemistry 270 (8): 3506–11. February 1995. doi:10.1074/jbc.270.8.3506. PMID 7876084.
- ↑ "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 Physiology 123 (4): 1437–48. August 2000. doi:10.1104/pp.123.4.1437. PMID 10938360.
- ↑ "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 Physiology 122 (4): 1311–21. April 2000. doi:10.1104/pp.122.4.1311. PMID 10759528.
- ↑ "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiology 129 (3): 1222–31. July 2002. doi:10.1104/pp.000687. PMID 12114576.
- ↑ "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome". Proceedings of the National Academy of Sciences of the United States of America 102 (5): 1779–84. February 2005. doi:10.1073/pnas.0409233102. PMID 15665094. Bibcode: 2005PNAS..102.1779K.
External links
- Tyrosine+N-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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