کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10759226 | 1050417 | 2013 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Substrate specificity of undecaprenyl diphosphate synthase from the hyperthermophilic archaeon Aeropyrum pernix
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کلمات کلیدی
FPPDMAPPGPPIPPGGPPIsoprenoid - ایسپرونیدisopentenyl diphosphate - ایسپنتنیل دی فسفاتArchaea - باستانیان یا آرکیاUpP - بالاdimethylallyl diphosphate - دی متیللید دی فسفاتfarnesyl diphosphate - فارسیل دی فسفاتPrenyltransferase - پرنیل ترانسفرازGeranyl diphosphate - ژانایل دی فسفاتgeranylgeranyl diphosphate - گوارانیلگرانیل دی فسفات
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cis-prenyltransferase from a hyperthermophilic archaeon Aeropyrum pernix was expressed in Escherichia coli and purified for characterization. Properties such as substrate specificity, product chain-length, thermal stability and cofactor requirement were investigated using the recombinant enzyme. In particular, the substrate specificity of the enzyme attracts interest because only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate in A. pernix. From the enzymatic study, the archaeal enzyme was shown to be undecaprenyl diphosphate synthase that has anomalous substrate specificity, which results in a preference for geranylfarnesyl diphosphate. This means that the product of the enzyme, which is probably used as the precursor of the glycosyl carrier lipid, would have an undiscovered structure.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 436, Issue 2, 28 June 2013, Pages 230-234
Journal: Biochemical and Biophysical Research Communications - Volume 436, Issue 2, 28 June 2013, Pages 230-234
نویسندگان
Takeshi Mori, Takuya Ogawa, Tohru Yoshimura, Hisashi Hemmi,