Izoflavon 7-O-metiltransferaza
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
| 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 | ||||||||
| |||||||||
- S-adenozil-L-metionin + 7-hidroksiizoflavon 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
uredi- ↑ Edwards, R. and Dixon, R.A. (1991). „Isoflavone O-methyltransferase activities in elicitor-treated cell suspension cultures of Medicago sativa”. Phytochemistry 30: 2597-2606.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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
uredi- 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.