Heterologous expression, biochemical characterisation and computational analysis of Bacteroides fragilis enolase


Ugurel E., Kocer S., Sariyer E., MUTLU Ö., Inci T. G. , Ugurel O. M. , ...More

Computational Biology and Chemistry, vol.98, 2022 (Journal Indexed in SCI Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 98
  • Publication Date: 2022
  • Doi Number: 10.1016/j.compbiolchem.2022.107658
  • Title of Journal : Computational Biology and Chemistry
  • Keywords: Antibiotic resistance, Bacteriodes fragilis, Enolase, Enzyme kinetic, In silico studies, Structure-based drug design

Abstract

© 2022Bacteriodes fragilis is an anaerobic bacterium found in the human intestinal flora. In this study, BfEno was targeted with a structure-based drug design approach because inhibition of this enzyme may prevent both the aerobic and anaerobic pathways due to its role in the glycolytic pathway. First, the gene encoding BfEno was cloned, expressed and the protein produced over 95% purity. The Km and Vmax values of BfEno were determined as 314.9 µM and 256.2 µmol/min.mg, respectively. Drug-like chemicals were retrieved from the ZINC database for high-throughput virtual screening analyses. As a result of screening study, the ZINC91441604 has been proposed to bind to the active site of the enzyme and remain stable. The same compound exhibited weak binding to the human enolases than the bacterial enolase. Hence, ZINC91441604 may be proposed as a novel candidate for further in vitro and in vivo drug analysis towards the treatment of B. fragilis infections.