کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10883719 | 1078597 | 2005 | 46 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes
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کلمات کلیدی
Humicola griseaCBMPNPCTrichoderma reeseiNAGNCSCBHT. reeseiHypocrea jecorina - jecorina HYPOCREAN-Acetyl-Glucosamine - N-استیل گلوکوزامینEndoglucanase - اندوگلیکونازnon-crystallographic symmetry - تقارن غیر کریستالوگرافیCatalytic domain - دامنه کاتالیستیdegree of polymerization - درجه پلیمریزاسیونcircular dichroism - رنگ تابی دورانیProtein structure - ساختار پروتئینCellobiose - سلبیوزCellotetraose - سلوتورتوزcellobiohydrolase - سلولی بیو هیدرولازCellopentaose - سلپنتوزcellulose binding module - ماژول اتصال سلولزProtein engineering - مهندسی پروتئینwild type - نوع وحشیThermal stability - پایداری حرارتیGliocladium roseum - گلیوکادیوم رزومهglycoside hydrolase - گلیکوزید هیدرولاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوفیزیک
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In this review we will describe how we have gathered structural and biochemical information from several homologous cellulases from one class of glycoside hydrolases (GH family 12), and used this information within the framework of a protein-engineering program for the design of new variants of these enzymes. These variants have been characterized to identify some of the positions and the types of mutations in the enzymes that are responsible for some of the biochemical differences in thermal stability and activity between the homologous enzymes. In this process we have solved the three-dimensional structure of four of these homologous GH 12 cellulases: Three fungal enzymes, Humicola grisea Cel12A, Hypocrea jecorina Cel12A and Hypocrea schweinitzii Cel12A, and one bacterial, Streptomyces sp. 11AG8 Cel12A. We have also determined the three-dimensional structures of the two most stable H. jecorina Cel12A variants. In addition, four ligand-complex structures of the wild-type H. grisea Cel12A enzyme have been solved and have made it possible to characterize some of the interactions between substrate and enzyme. The structural and biochemical studies of these related GH 12 enzymes, and their variants, have provided insight on how specific residues contribute to protein thermal stability and enzyme activity. This knowledge can serve as a structural toolbox for the design of Cel12A enzymes with specific properties and features suited to existing or new applications.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Progress in Biophysics and Molecular Biology - Volume 89, Issue 3, November 2005, Pages 246-291
Journal: Progress in Biophysics and Molecular Biology - Volume 89, Issue 3, November 2005, Pages 246-291
نویسندگان
Mats Sandgren, Jerry Ståhlberg, Colin Mitchinson,