کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7561198 | 1491450 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Insight into the binding of the wild type and mutated alginate lyase (AlyVI) with its substrate: A computational and experimental study
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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![عکس صفحه اول مقاله: Insight into the binding of the wild type and mutated alginate lyase (AlyVI) with its substrate: A computational and experimental study Insight into the binding of the wild type and mutated alginate lyase (AlyVI) with its substrate: A computational and experimental study](/preview/png/7561198.png)
چکیده انگلیسی
The homology model of the wild type alginate lyase (AlyVI) marine bacterium Vibrio sp. protein, was built using the crystal structure of the Family 7 alginate lyase from Sphingomonas sp. A1. To rationalize the observed structure-affinity relationships of aliginate lyase alyVI with its (GGG) substrate, molecular docking, MD imulations and binding free energy calculations followed by site-directed mutagenesis and alyVI activity assays were carried out. Per-residue decomposition of the (GGG) binding energy revealed that the most important contributions were from polar and charged residues, such as Asn138, Arg143, Asn217, and Lys308, while van der Waals interactions were responsible for binding with the catalytic His200 and Tyr312 residues. The mutants H200A, K308A, Y312A, Y312F, and W165A were found to be inactive or almost inactive. However, the catalytic efficiency (kcat/Km) of the double mutant L224V/D226G increased by two-fold compared to the wild type enzyme. This first structural model with its substrate binding mode and the agreement with experimental results provide a suitable base for the future rational design of new mutated alyVI structures with improved catalytic activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1814, Issue 12, December 2011, Pages 1739-1747
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1814, Issue 12, December 2011, Pages 1739-1747
نویسندگان
Adel Hamza, Yu Lan Piao, Mi-Sun Kim, Cheol Hee Choi, Chang-Guo Zhan, Hoon Cho,