1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
Investigation of the mechanism of phenol inhibitory activity in the function of fructosyl peptide oxidase
Paper ID : 1299-ICB10
Authors:
Mona Masoumparast *, Amirreza Farajnezhadi, Mehran Habibi-Rezaei
Protein Biotechnology Research Lab (PBRL), School of Biology, University of Tehran, Tehran, Iran.
Abstract:
Fructosyl peptide oxidase (FPOX, EC: 1.5.3) that belongs to the oxidoreductase family can identify fructosyl valine (FV) and fructosyl lysine (FK) as substrate. In this reaction, fructosyl amino acids are broken into glucosone, amino acids, and hydrogen peroxide (H2O2). The amount of produced H2O2 measures reacted substrate that could be monitored with colorimetric methods.[1] As a measurement method, 4-aminoantipyrine and phenol act as electron scavengers to adsorb free radicals produced by H2O2 in the presence of peroxidase. [2][3] It was observed in laboratory studies that a high phenol concentration could interfere with FPOX activity. Therefore, we conducted an in silico study to discover the phenol inhibition activity. Firstly, FPOX (PDB ID: 4RSL) active sites and pockets were identified by the Computed Atlas of Surface Topography of proteins (CASTp). Then Auto Dock Vina was employed to investigate the binding of FK and phenol to the FPOX. Accordingly, the binding affinities of the FK and phenol to the FPOX active site were calculated as -23.87 and -21.35 kJ/mol, respectively. These results suggested that phenol could not interfere with the enzyme’s function, especially in low concentrations. Although, when phenol concentration increases, it can compete with FK for binding FPOX active site to inhibit its activity possibly in a competitive manner of action.
Keywords:
Fructosyl peptide oxidase; Enzyme Activity; Molecular docking; Phenol.
Status : Paper Accepted (Poster Presentation)