An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.

ABSTRACT: One third of all drugs in clinical use owe their pharmacological activity to the functional inhibition of enzymes, highlighting the importance of enzymatic targets for drug development. Because of the close relationship between inhibition and catalysis, understanding the recognition and turnover of enzymatic substrates is essential for rational drug design. Although the Staphylococcus aureus enoyl-acyl carrier protein reductase (saFabI) involved in bacterial fatty acid biosynthesis constitutes a very promising target for the development of novel, urgently needed anti-staphylococcal agents, the substrate binding mode and catalytic mechanism remained unclear for this enzyme. Using a combined crystallographic, kinetic, and computational approach, we have explored the chemical properties of th

SUBMITTER: Schiebel J 

PROVIDER: S-EPMC4382590 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature