کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1178422 | 962691 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Tyrosine83 is essential for the activity of E. coli galactoside transacetylase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
The gene (lacA) coding for Escherichia coli galactoside transacetylase was cloned into the pTrcHisB plasmid, and the corresponding hexahistidine-tagged enzyme was over-expressed and purified. The kinetic constants of the tagged protein were determined, yielding values in excellent agreement with previous observations reported for the natural enzyme. LacA Tyrosine83 was then substituted with a Valine: by comparing the Km and kcat values observed for wild type and mutant enzymes using isopropyl-thio-β-d-galactopyranoside or p-nitrophenyl-β-d-galactopyranoside as substrates, Tyrosine83 was identified as an essential residue for the catalytic activity of E. coli galactoside transacetylase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1774, Issue 2, February 2007, Pages 243–248
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1774, Issue 2, February 2007, Pages 243–248
نویسندگان
A. Radeghieri, M. Bonoli, F. Parmeggiani, A. Hochkoeppler,