Tirozin N-monooksigenaza

Tirozin N-monooksigenaza
Identifikatori
EC broj	1.14.13.41
CAS broj	159447-19-5
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga PMC articles PubMed articles NCBI Protein search

Tirozin N-monooksigenaza (EC 1.14.13.41, tirozinska N-hidroksilaza, CYP79A1) je enzim sa sistematskim imenom L-tirozin,NADPH:kiseonik oksidoreduktaza (N-hidroksilacija).^{[1][2][3][4][5][6]} Ovaj enzim katalizuje sledeću hemijsku reakciju

L-tirozin + 2 O₂ + 2 NADPH + 2 H⁺ ${\displaystyle \rightleftharpoons }$ (Z)-[4-hidroksifenilacetaldehid oksim] + 2 NADP⁺ + CO₂ + 3H₂O (sveukupna reakcija)

(1a) L-tirozin + O₂ + NADPH + H⁺ ${\displaystyle \rightleftharpoons }$ N-hidroksi-L-tirozin + NADP⁺ + H₂O

(1b) N-hidroksi-L-tirozin + O₂ + NADPH + H⁺ ${\displaystyle \rightleftharpoons }$ N,N-dihidroksi-L-tirozin + NADP⁺ + H₂O

(1c) N,N-dihidroksi-L-tirozin ${\displaystyle \rightleftharpoons }$ (Z)-[4-hidroksifenilacetaldehid oksim] + CO₂ + H₂O

Ovaj enzim je hem-tiolatni protein (P-450). On učestvuje u biosintezi cijanogenog glukozida dhurina.

Reference

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: 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: 3506-3511. 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: 1437-1448. 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. 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. 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. PMID 15665094. 

Literatura

• Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
• Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
• Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
• Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
• Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
• Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Vanjske veze

• MeSH Tyrosine+N-monooxygenase