کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10770402 | 1050833 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Enzymatic and structural characterization of type II isopentenyl diphosphate isomerase from hyperthermophilic archaeon Thermococcus kodakaraensis
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Enzymatic and thermodynamic characteristics of type II isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase (Tk-IDI) from Thermococcus kodakaraensis, which catalyzes the interconversion of IPP and DMAPP, were examined. FMN was tightly bound to Tk-IDI, and the enzyme required NADPH and Mg2+ for the isomerization in both directions. The melting temperature (Tm), the change of enthalpy (ÎHm), and the heat capacity change (ÎCp) of Tk-IDI were 88.0 °C, 444 kJ molâ1, and 13.2 kJ molâ1 Kâ1, respectively, indicating that Tk-IDI is fairly thermostable. Kinetic parameters dramatically changed when the temperature crossed 80 °C even though its native overall structure was stably maintained up to 90 °C, suggesting that local conformational change would occur around 80 °C. This speculation was supported by the result of the circular dichroism analysis that showed the shift of the α-helical content occurred at 80 °C.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 4, 17 June 2005, Pages 1127-1136
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 4, 17 June 2005, Pages 1127-1136
نویسندگان
Masood Ahmed Siddiqui, Aiko Yamanaka, Kazutake Hirooka, Takeshi Bamaba, Akio Kobayashi, Tadayuki Imanaka, Ei-ichiro Fukusaki, Shinsuke Fujiwara,