کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1936589 | 1050695 | 2008 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP
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کلمات کلیدی
Nbs2d-glyceraldehyde-3-phosphateAMP-PCP1,3-BPGEnantioselectivityDTTPGKGAPDHDSC1,3-bisphosphoglycerateAMP-PNP3-PG3-phosphoglycerate - 3-فسفوگلسراتdithiothreitol - دیتیوتریتولGAP - شکافinorganic phosphate - فسفات معدنیMicrocalorimetry - میکروکالوریمتریhuman immunodeficiency virus - ویروس نقص ایمنی انسانیHIV - ویروس نقص ایمنی انسانی small angle X-ray Scattering - پراکندگی اشعه ایکس زاویه کوچکDifferential scanning calorimetry - کالریمتری روبشی افتراقی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP](/preview/png/1936589.png)
چکیده انگلیسی
l-Nucleoside-analogues, mirror images of the natural d-nucleosides, are a new class of antiviral and anticancer agents. In the cell they have to be phosphorylated to pharmacologically active triphosphate forms, the last step seems to involve human 3-phosphoglycerate kinase (hPGK). Here we present a steady state kinetic and biophysical study of the interaction of the model compound l-MgADP with hPGK. l-MgADP is a good substrate with kcat and Km values of 685Â sâ1 and 0.27Â mM, respectively. Double inhibition studies suggest that l-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation, as detected by microcalorimetry. Structural details of the interaction in the enzyme active site are different for the d- and l-enantiomers (e.g. the effect of Mg2+), but these differences do not prevent the occurrence of the catalytic cycle, which is accompanied by the hinge-bending domain closure, as indicated by SAXS measurements.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 366, Issue 4, 22 February 2008, Pages 994-1000
Journal: Biochemical and Biophysical Research Communications - Volume 366, Issue 4, 22 February 2008, Pages 994-1000
نویسندگان
Andrea Varga, Judit Szabó, Beáta Flachner, Béatrice Roy, Peter Konarev, Dmitri Svergun, Péter Závodszky, Christian Périgaud, Tom Barman, Corinne Lionne, Mária Vas,