Tyrosine N-monooxygenase

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Tyrosine N-monooxygenase
Tyrosine N-monooxygenase
Identifiers
EC no.	1.14.13.41
CAS no.	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
PMC
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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

^ Halkier BA, Møller BL (December 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". The Journal of Biological Chemistry. 265 (34): 21114–21. doi:10.1016/S0021-9258(17)45334-8. PMID 2250015.
^ Sibbesen O, Koch B, Halkier BA, Møller BL (February 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". The Journal of Biological Chemistry. 270 (8): 3506–11. doi:10.1074/jbc.270.8.3506. PMID 7876084.
^ Bak S, Olsen CE, Halkier BA, Møller BL (August 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 Physiology. 123 (4): 1437–48. doi:10.1104/pp.123.4.1437. PMC 59100. PMID 10938360.
^ Nielsen JS, Møller BL (April 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 Physiology. 122 (4): 1311–21. doi:10.1104/pp.122.4.1311. PMC 58967. PMID 10759528.
^ Busk PK, Møller BL (July 2002). "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiology. 129 (3): 1222–31. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.
^ Kristensen C, Morant M, Olsen CE, Ekstrøm CT, Galbraith DW, Møller BL, Bak S (February 2005). "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. Bibcode:2005PNAS..102.1779K. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.

External links

Tyrosine+N-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Halkier BA, Møller BL (December 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". The Journal of Biological Chemistry. 265 (34): 21114–21. doi:10.1016/S0021-9258(17)45334-8. PMID 2250015.

[2] Sibbesen O, Koch B, Halkier BA, Møller BL (February 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". The Journal of Biological Chemistry. 270 (8): 3506–11. doi:10.1074/jbc.270.8.3506. PMID 7876084.

[3] Bak S, Olsen CE, Halkier BA, Møller BL (August 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 Physiology. 123 (4): 1437–48. doi:10.1104/pp.123.4.1437. PMC 59100. PMID 10938360.

[4] Nielsen JS, Møller BL (April 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 Physiology. 122 (4): 1311–21. doi:10.1104/pp.122.4.1311. PMC 58967. PMID 10759528.

[5] Busk PK, Møller BL (July 2002). "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiology. 129 (3): 1222–31. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.

[6] Kristensen C, Morant M, Olsen CE, Ekstrøm CT, Galbraith DW, Møller BL, Bak S (February 2005). "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. Bibcode:2005PNAS..102.1779K. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.

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