Izoflavon 7-O-metiltransferaza

Izoflavon 7-O-metiltransferaza
Identifikatori
EC broj	2.1.1.150
CAS broj	136111-54-1
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

Izoflavon 7-O-metiltransferaza (EC 2.1.1.150) je enzim sa sistematskim imenom S-adenozil-L-metionin:hidroksiizoflavon 7-O-metiltransferaza.^{[1][2][3][4][5][6]} Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + 7-hidroksiizoflavon ${\displaystyle \rightleftharpoons }$ S-adenozil-L-homocistein + 7-metoksiizoflavon

Enzim iz lucerke može da metiliše daidzein, genistein i 6,7,4'-trihidroksiizoflavon. On nije aktivan na flavonima i flavanonima.

Reference

1. Edwards, R. and Dixon, R.A. (1991). „Isoflavone O-methyltransferase activities in elicitor-treated cell suspension cultures of Medicago sativa”. Phytochemistry 30: 2597-2606. 
2. He, X.Z. and Dixon, R.A. (2000). „Genetic manipulation of isoflavone 7-O-methyltransferase enhances biosynthesis of 4′-O-methylated isoflavonoid phytoalexins and disease resistance in alfalfa”. Plant Cell 12: 1689-1702. PMID 11006341. 
3. He, X.-Z. and Dixon, R.A. (1996). „Affinity chromatography, substrate/product specificity, and amino acid sequence analysis of an isoflavone O-methyltransferase from alfalfa (Medicago sativa L.)”. Arch. Biochem. Biophys. 336: 121-129. PMID 8951042. 
4. He, X.Z., Reddy, J.T. and Dixon, R.A. (1998). „Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and characterization of an elicitor-inducible isoflavone 7-O-methyltransferase”. Plant Mol. Biol. 36: 43-54. PMID 9484461. 
5. Liu, C.-J. and Dixon, R.A. (2001). „Elicitor-induced association of isoflavone O-methyltransferase with endomembranes prevents the formation and 7-O-methylation of daidzein during isoflavonoid phytoalexin biosynthesis”. Plant Cell 13: 2643-2658. PMID 11752378. 
6. Zubieta, C., He, X.-Z., Dixon, R.A. and Noel, J.P. (2001). „Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases”. Nat. Struct. Biol. 8: 271-279. PMID 11224575. 

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 Isoflavone+7-O-methyltransferase