کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1361052 | 981456 | 2008 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic parameters and recognition of thymidine analogues with varying functional groups by thymidine phosphorylase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Thymidine phosphorylase (TP, EC 2.4.2.4) recognized the structure of the substrate with high specificity, via both the base and the ribosyl moieties. The replacement of 3â²-OH of thymidine markedly influenced its catalytic activity with TP. The conversion of pyrimidine nucleosides with modified base moieties to the corresponding 1-phosphate form was poor. The leaving group activity decreased with an increase in aromaticity of the pyrimidine base moiety, because of increased difficulty in polarizing the base by the amino acids local to the active site. The replacement of 3â² and 5â² functional groups tended to decrease the reaction rate and the percentage conversion with TP. In particular the ribosyl 3â² hydroxyl group was structurally important for the binding of the substrate by the enzyme. The kinetic assay clearly showed high Km and low Vmax values on replacing the 3â² hydroxyl group with hydrogen.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry - Volume 16, Issue 7, 1 April 2008, Pages 3866-3870
Journal: Bioorganic & Medicinal Chemistry - Volume 16, Issue 7, 1 April 2008, Pages 3866-3870
نویسندگان
Akihiko Hatano, Aiko Harano, Yoshikatsu Takigawa, Yasuhiro Naramoto, Keisuke Toda, Yuuichi Nakagomi, Hideyuki Yamada,