TY  - JOUR
N1  - OPEN ACCESS
ID  - open465
UR  - http://www.biomedcentral.com/content/pdf/1471-2091-12-31.pdf
A1  - Banerjee, Shrijita
A1  - Ekka, Mary Krishna
A1  - Kumaran, Sangaralingam
Y1  - 2011///
N2  - 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.
PB  - Biomedcentral
JF  - BMC biochemistry
VL  - 12
KW  - Ligand Binding
KW  -  Enthalpy
KW  -  Entropy
KW  -  Fluorescence
KW  -  Isothermal Titration Calorimetry
SN  - 1471-2091
TI  - Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
AV  - public
ER  -