کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10870000 | 1073985 | 2015 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase
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کلمات کلیدی
HPAEC-PADCGTaseTransglucosylationpNPGBSA - BSAbovine serum albumin - آلبومین سرم گاوAmylosucrase - آمیلوسوکراسGlycoside hydrolase family 13 - خانواده هیدرولاز گلیکوزید 13Acceptor specificity - خصوصیات پذیرندهcyclodextrin glucanotransferase - سیکلوکودکسترین گلوکانوتانسفرازhigh performance anion exchange chromatography with pulsed amperometric detection - کروماتوگرافی مبدل آنیون با عملکرد بالا با تشخیص آمپومتریک پالسglycoside hydrolase - گلیکوزید هیدرولاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase](/preview/png/10870000.png)
چکیده انگلیسی
Streptococcus mutans dextran glucosidase (SmDG) belongs to glycoside hydrolase family 13, and catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form α-(1 â 6)-glucosidic linkage at the substrate non-reducing ends. Here, we report the 2.4 Ã
resolution crystal structure of glucosyl-enzyme intermediate of SmDG. In the obtained structure, the Trp238 side-chain that constitutes the substrate-binding site turned away from the active pocket, concurrently with conformational changes of the nucleophile and the acid/base residues. Different conformations of Trp238 in each reaction stage indicated its flexibility. Considering the results of kinetic analyses, such flexibility may reflect a requirement for the reaction mechanism of SmDG.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 589, Issue 4, 13 February 2015, Pages 484-489
Journal: FEBS Letters - Volume 589, Issue 4, 13 February 2015, Pages 484-489
نویسندگان
Momoko Kobayashi, Wataru Saburi, Daichi Nakatsuka, Hironori Hondoh, Koji Kato, Masayuki Okuyama, Haruhide Mori, Atsuo Kimura, Min Yao,