کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2050992 1074187 2007 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: Implications for ligand binding sites
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: Implications for ligand binding sites
چکیده انگلیسی

Two phosphofructokinase (PFK) chimeras were constructed by exchanging the N- and C-terminal halves of the mammalian M- and C-type isozymes, to investigate the contribution of each terminus to the catalytic site and the fructose-2,6-P2/fructose-1,6-P2 allosteric site. The homogeneously-purified chimeric enzymes organized into tetramers, and exhibited kinetic properties for fructose-6-P and MgATP similar to those of the native enzyme that furnished the N-terminal domain in each case, whereas their fructose-2,6-P2 activatory characteristics coincided with those of the isozyme that provided the C-terminal half. This reflected the role of each domain in the formation of the corresponding binding site. Grafting the N-terminus of PFK-M onto the C-terminus of the fructose-1,6-P2 insensitive PFK-C restored transduction of this signal to the catalytic site, which significance is also discussed.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 581, Issue 16, 26 June 2007, Pages 3033–3038
نویسندگان
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