کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2049215 1074120 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Determination of substrate binding energies in individual subsites of a family 18 chitinase
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Determination of substrate binding energies in individual subsites of a family 18 chitinase
چکیده انگلیسی

Thermodynamic parameters for binding of N-acetylglucosamine (GlcNAc) oligomers to a family 18 chitinase, ChiB of Serratia marcescens, have been determined using isothermal titration calorimetry. Binding studies with oligomers of different lengths showed that binding to subsites −2 and +1 is driven by a favorable enthalpy change, while binding to the two other most important subsites, +2 and +3, is driven by entropy with unfavorable enthalpy. These remarkable unfavorable enthalpy changes are most likely due to favorable enzyme-substrate interactions being offset by unfavorable enthalpic effects of the conformational changes that accompany substrate-binding.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 584, Issue 22, 19 November 2010, Pages 4581–4585
نویسندگان
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