کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10870300 | 1073997 | 2015 | 31 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
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کلمات کلیدی
DSCPNAPNBPnOp-nitrophenyl butyrate - p-nitrofenyl butyratep-Nitrophenyl acetate - p-نیترفنیل استاتSaccharification - تبدیل به قند یا قندسازیXylanase - زایلانازBiomass - زیست توده یا بیومسCatalytic triad - سه گانه کاتالیستیDisulfide bond - پیوند دی سولفیدDifferential scanning calorimetry - کالریمتری روبشی افتراقیcarbohydrate esterase - کربوهیدرات استراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site](/preview/png/10870300.png)
چکیده انگلیسی
Carbohydrate esterase catalyzes the de-O or de-N-acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from Talaromyces cellulolyticus. Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5Â Ã
resolution. From the structural analysis, it was elucidated that a n-octyl-β-d-glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site-directed mutagenesis showed that the N-terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 589, Issue 11, 8 May 2015, Pages 1200-1206
Journal: FEBS Letters - Volume 589, Issue 11, 8 May 2015, Pages 1200-1206
نویسندگان
Masahiro Watanabe, Harumi Fukada, Hiroyuki Inoue, Kazuhiko Ishikawa,