کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1178338 | 962684 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
6His–Eco29kI methyltransferase methylation site and kinetic mechanism characterization
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
A new type II 6His–Eco29kI DNA methyltransferase was tested for methylation site (CCMeGCGG) and catalytic reaction optimal conditions. With high substrate concentrations, an inhibitory effect of DNA, but not AdoMet, on its activity was observed. Isotope partitioning and substrate preincubation assays showed that the enzyme–AdoMet complex is catalytically active. Considering effect of different concentrations of DNA and AdoMet on initial velocity, ping-pong mechanisms were ruled out. According to data obtained, the enzyme appears to work by preferred ordered bi–bi mechanism with AdoMet as leading substrate.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1774, Issue 8, August 2007, Pages 1014–1019
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1774, Issue 8, August 2007, Pages 1014–1019
نویسندگان
Dmitri Nikitin, Marina Mokrishcheva, Alexander Solonin,