کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
674318 1459557 2012 4 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Subsite binding energies of an exo-polygalacturonase using isothermal titration calorimetry
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی جریان سیال و فرایندهای انتقال
پیش نمایش صفحه اول مقاله
Subsite binding energies of an exo-polygalacturonase using isothermal titration calorimetry
چکیده انگلیسی

Thermodynamic parameters for binding of a series of galacturonic acid oligomers to an exo-polygalacturonase, RPG16 from Rhizopus oryzae, were determined by isothermal titration calorimetry. Binding of oligomers varying in chain length from two to five galacturonic acid residues is an exothermic process that is enthalpically driven and results in extremely tight binding of the substrate to RPG16. Binding energies in combination with prior biochemical data suggests that RPG16 has the potential for five subsites, −1 to +4, with the greatest contribution to binding energies arising from subsite −1/+1. While the enthalpic contribution to binding decreases substantially for subsites +2 to +4, beneficial entropic effects occur in subsites +3 and +4 leading to increased total free energy as the length of oligomer increases. This information will be useful for additional studies in determining the binding contributions of specific amino acids with mutant enzymes.


► Thermodynamics of (GalpA)n oligomers binding to an exo-polygalacturonase.
► Energetics of binding (GalpA)n were determined by ITC.
► Thermodynamic parameters attributable to individual subsites were determined.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Thermochimica Acta - Volume 527, 10 January 2012, Pages 219–222
نویسندگان
, , ,