کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882066 | 1536535 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mutation in the flexible loop of 1-deoxy-d-xylulose 5-phosphate reductoisomerase broadens substrate utilization
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Mutation in the flexible loop of 1-deoxy-d-xylulose 5-phosphate reductoisomerase broadens substrate utilization Mutation in the flexible loop of 1-deoxy-d-xylulose 5-phosphate reductoisomerase broadens substrate utilization](/preview/png/9882066.png)
چکیده انگلیسی
The second enzyme in the methylerythritol phosphate pathway to isoprenoids, 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR; EC 1.1.1.267) mediates the transformation of 1-deoxy-d-xylulose 5-phosphate (DXP) into 2-C-methyl-d-erythritol 4-phosphate. Several DXR mutants have been prepared to study amino acid residues important in binding or catalysis, but in-depth studies of many conserved residues in the flexible loop portion of the enzyme have not been conducted. In the course of our studies of this enzyme, an analog of DXP, 1,2-dideoxy-d-threo-3-hexulose 6-phosphate (1-methyl-DXP), was found to be a weak competitive inhibitor. Using the X-ray crystal structures of DXR as a guide, a highly conserved tryptophan residue in the flexible loop was identified that potentially blocks the use of this analog as a substrate. To test this hypothesis, four mutants of the Synechocystis sp. PCC6803 DXR were prepared and a W204F mutant was found to utilize the analog as a substrate.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 2, 15 December 2005, Pages 159-164
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 2, 15 December 2005, Pages 159-164
نویسندگان
Roberta P.M. Fernandes, Chanokporn Phaosiri, Philip J. Proteau,