%0 Journal Article
%@ 1471-2091
%A Banerjee, Shrijita
%A Ekka, Mary Krishna
%A Kumaran, Sangaralingam
%D 2011
%F open:465
%I Biomedcentral
%J BMC biochemistry
%K Ligand Binding, Enthalpy, Entropy, Fluorescence, Isothermal Titration Calorimetry
%P 31
%T Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
%U http://crdd.osdd.net/open/465/
%V 12
%X We show that OASS from three different pathogenic bacteria bind substrate and product through two different mechanisms. Results indicate that predominantly entropy driven methionine binding is not mediated through classical hydrophobic binding, instead, may involve desolvation of the polar active site. We speculate that OASS in general, may exhibit two different binding mechanisms for recognizing substrates and products.
%Z OPEN ACCESS