European Journal of Biomedical and Pharmaceutical Sciences

CAPTURING THE STRUCTURAL VARIATION OF 1-PHOSPHOFRUCTOKINASE FROM DIFFERENT PATHOGENIC BACTERIA: AN IN SILICO APPROACH

Dr. Ayon Pal*

ABSTRACT

The enzyme phosphofructokinase (PFK) plays a vital role in the linear EMP glucose degradation pathway where it catalyzes an important rate determining step, the phosphorylation of fructose-6-phosphate to fructose-1,6- bisphosphate. In this study, a relative analysis of the PFK protein sequences and tertiary structures have been carried out from a few plant and human pathogenic eubacteria to capture how the amino acid compositional fluctuation has transpired into structural variation. Phylogenetic analysis of the PFK protein sequences was also carried out using Bayesian approach. Analysis of the protein sequence as well as the structural features of PFK from different pathogenic eubacterial species suggest that the enzyme has evolved in a polyphletic manner and has undergone variable evolutionary change. In terms of evolutionary change, the PFK enzyme of Staphylococcus aureus and Streptococcus pneumoniae was found to demonstrate the least amount of change. The PFK enzyme of Clostridium perfringens was found to be quite unique, both in terms of amino acid composition and structural features from the remaining eubacterial species considered in this study.

Keywords: Phosphofructokinase, protein modeling, RMSD, multiple sequence alignment, phylogenetics, Bayesian inference, structural alignment, pathogenic bacteria.