The effect of glycosylation on the chloroperoxidase structure: A molecular dynamic simulation analysis

Chloroperoxidase (CPO), a heme-thiolate protein secreted by the marine fungus Caldariomyces fumago, has received much attention as the most versatile known heme enzyme. The signature function of CPO is halogenation of electron-rich organic substrates [1]. Chloroperoxidase is an extensively glycosylated monomeric enzyme with both N- and O-linked glycosyl chains [2]. Molecular dynamics (MD) simulations were performed by the GROMACS 4.5.6 package using the GROMOS96 43A1 force field [3]. In this study, the effect of glycosylation on the structure of chloroperoxidase has been investigated using MD simulation. Root mean square deviation (RMSD), root mean square fluctuation (RMSF) and protein secondary structure were evaluated before and after the removal of the carbohydrate. The results of RMSD showed that glycosylated enzyme increases stability rather than unglycosylated enzyme. RMSF values revealed that the flexibility of most residuals of enzyme reduces after removing N-linked oligosaccharides from CPO. The analysis of secondary structure showed that glycosylation on the chloroperoxidase reduces the formation of 3.10 Helix in the structure of protein. This study confirmed the experimental results of the role of N- and O-linked glycosyl chains in the structure and function of CPO.

کلیدواژه ها:

Chloroperoxidase ، glycosylation ، Molecular dynamics