Abstract
Molecular docking of polyhydroxy substituted flavone analogues (1-25) as substrate molecules to the active site of tyrosinase (PDB ID: Deoxy-form (2ZMX) & Oxy-form (1WX2)) and Free-Wilson analysis were studied to understand the roles of hydroxyl substituents (R_1-R_9) in substrate molecules for the tyrosinase inhibitory activation. It is founded from Free-Wilson analysis that the R_1=hydroxyl among R_1-R_9 substituents had the strongest influence on the tyrosinase inhibitory activity. H-bonds between the hydroxyl substituents of substrate molecules and amino acid residues in the active site of tyrosinase were contributed to make a stable substrate-receptor complex compound. Particularly, it is proposed from the findings that the noncompetitive inhibitory activation would take place via H-bonding between peroxide oxygen (Per404) atom in the active site of tyrosinase and the hydroxyl substituents in substrate molecule.
| Translated title of the contribution | The Roles of Hydroxyl Substituents in Tyrosinase Inhibitory Activation of Flavone Analogues |
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| Original language | Korean |
| Pages (from-to) | 56-62 |
| Number of pages | 7 |
| Journal | Journal of Applied Biological Chemistry |
| Volume | 54 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2011 |