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
Search PMC articles PubMed articles NCBI proteins

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⁺ $\rightleftharpoons$ (Z)-[4-hydroxyphenylacetaldehyde oxime] + 2 NADP⁺ + CO₂ + 3 H₂O (overall reaction)

(1a) L-tyrosine + O₂ + NADPH + H⁺ $\rightleftharpoons$ N-hydroxy-L-tyrosine + NADP⁺ + H₂O

(1b) N-hydroxy-L-tyrosine + O₂ + NADPH + H⁺ $\rightleftharpoons$ N,N-dihydroxy-L-tyrosine + NADP⁺ + H₂O

(1c) N,N-dihydroxy-L-tyrosine $\rightleftharpoons$ (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO₂ + H₂O

Tyrosine N-monooxygenase is heme-thiolate protein (P-450).

References

1. Halkier, B.A. and 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.
2. Sibbesen, O., Koch, B., Halkier, B.A. and 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.
3. Bak, S., Olsen, C.E., Halkier, B.A. and 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.
4. Nielsen, J.S. and 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.
5. Busk, P.K. and 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.
6. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and 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)