Sucrose Phosphorylase Harbouring a Redesigned, Glycosyltransferase-Like Active Site Exhibits Retaining Glucosyl Transfer in the Absence of a Covalent Intermediate

被引:27
作者
Goedl, Christiane [1 ]
Nidetzky, Bernd [1 ]
机构
[1] Graz Univ Technol, Inst Biotechnol & Biochem Engn, A-8010 Graz, Austria
基金
奥地利科学基金会;
关键词
glycosides; glycosyltransferases; molecular mechanisms; phosphorylases; structure-activity relationships; ALPHA-GALACTOSYLTRANSFERASE; BASE CATALYSIS; MUTANT; MECHANISM; INSIGHTS; DONOR; STATE; ACID;
D O I
10.1002/cbic.200900429
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
(Figure Presented) Mechanism makeover: We remodeled sucrose phosphorylase to mimic the active-site characteristics of a retaining glycosyltransferase. Thus, an enzymatic reaction coordinate for α-retaining glucosyl transfer through a covalent β-glucosyl enzyme intermediate was changed into one in which configurational retention appeared to be achieved through a direct front-side nucleophilic displacement reaction. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码:2333 / 2337
页数:5
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