English  |  正體中文  |  简体中文  |  Items with full text/Total items : 26988/38789
Visitors : 2350141      Online Users : 31
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39254

Title: Identification of Substrate-Binding and Selectivity-Related Residues of Maltooligosyltrehalose Synthase from the Thermophilic Archaeon Sulfolobus solfataricus ATCC 35092
Authors: Wen-Chi Tseng
Chia-Ray Lin
Xing-Guang Hung
Tsen-Yun Wei
Yu-Chun Chen
Tsuei-Yun Fang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: Maltooligosyltrehalose synthase
Hydrogen bond
Site-directed mutagenesis
Selectivity
Computer simulation
Sulfolobus
Date: 2014-03
Issue Date: 2016-11-30T07:51:57Z
Publisher: Enzyme and Microbial Technology
Abstract: Abstract: Maltooligosyltrehalose synthase (MTSase) is a key enzyme in the synthesis of trehalose. Computer simulations using AutoDock and NAMD were employed to assess the substrate-binding and selectivity-related residues of MTSase. We introduced mutations at residues D411, D610, and R614 to determine the substrate-binding residues of Sulfolobus solfataricus ATCC 35092 MTSase, and introduced mutations at residues P402, A406, and V426 to investigate the enzyme's selectivity-related residues. Kinetic studies of D411A, D610A, and R614A MTSases reveal significant reductions in catalytic efficiency and cause increase in the transition-state energy of mutant MTSases, indicating that residues D411, D610, and R614 form hydrogen bonds to the substrate. Compared with wild-type MTSase, the hydrolysis: transglycosylation selectivity ratio was significantly decreased for P402Q and significantly increased for A406S MTSases, while the ratio for V426T MTSase showed little change. The results suggest that P402 and A406 residues are selectivity-related.
Relation: 56(5)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39254
Appears in Collections:[食品科學系] 期刊論文

Files in This Item:

File Description SizeFormat
index.html0KbHTML40View/Open


All items in NTOUR are protected by copyright, with all rights reserved.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback