Tyrosine N-monooxygenase
| 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 | ||||||||
| |||||||||
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+ (Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP+ + CO2 + 3 H2O (overall reaction)
- (1a) L-tyrosine + O2 + NADPH + H+ N-hydroxy-L-tyrosine + NADP+ + H2O
- (1b) N-hydroxy-L-tyrosine + O2 + NADPH + H+ N,N-dihydroxy-L-tyrosine + NADP+ + H2O
- (1c) N,N-dihydroxy-L-tyrosine (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
Tyrosine N-monooxygenase is heme-thiolate protein (P-450).
References
- ↑ Halkier, B.A.; Møller, B.L. (1990). "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 (34): 21114–21121. PMID 2250015.
- ↑ Sibbesen, O.; Koch, B.; Halkier, B.A.; Møller, B.L. (1995). "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 (8): 3506–3511. doi:10.1074/jbc.270.8.3506. PMID 7876084.
- ↑ Bak, S.; Olsen, C.E.; Halkier, B.A.; Moller, B.L. (2000). "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 (4): 1437–1448. doi:10.1104/pp.123.4.1437. PMC 59100
. PMID 10938360. - ↑ Nielsen, J.S.; Moller, B.L. (2000). "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: 1311–1321. doi:10.1104/pp.122.4.1311. PMC 58967. PMID 10759528.
- ↑ Busk, P.K.; Møller, B.L. (2002). "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiol. 129: 1222–1231. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.
- ↑ Kristensen, C.; Morant, M.; Olsen, C.E.; Ekstrøm, C.T.; Galbraith, D.W.; Møller, B.L.; Bak, S. (2005). "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome". Proc. Natl. Acad. Sci. USA. 102: 1779–1784. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.
External links
- Tyrosine N-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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