Investigation of the mechanism of phenol inhibitory activity in the function of fructosyl peptide oxidase

Fructosyl peptide oxidase (FPOX, EC: ۱.۵.۳) that belongs to the oxidoreductase family can identify fructosylvaline (FV) and fructosyl lysine (FK) as substrate. In this reaction, fructosyl amino acids are broken intoglucosone, amino acids, and hydrogen peroxide (H۲O۲). The amount of produced H۲O۲ measures reactedsubstrate that could be monitored with colorimetric methods. As a measurement method, ۴-aminoantipyrineand phenol act as electron scavengers to adsorb free radicals produced by H۲O۲ in the presence of peroxidase.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 (PDBID: ۴RSL) 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 -۲۳.۸۷and -۲۱.۳۵ kJ/mol, respectively. These results suggested that phenol could not interfere with the enzyme’sfunction, especially in low concentrations. Although, when phenol concentration increases, it can competewith FK for binding FPOX active site to inhibit its activity possibly in a competitive manner of action.

کلیدواژه ها:

Fructosyl peptide oxidase ، Enzyme Activity ، Molecular docking ، Phenol