Structures of Maltohexaose and Maltoheptaose Bound at the Donor Sites of Cyclodextrin Glycosyltransferase Give Insight into the Mechanisms of Transglycosylation Activity and Cyclodextrin Size Specificity,-Reference-Cited by-同舟云学术

Structures of Maltohexaose and Maltoheptaose Bound at the Donor Sites of Cyclodextrin Glycosyltransferase Give Insight into the Mechanisms of Transglycosylation Activity and Cyclodextrin Size Specificity,

Published:2000-06-03 Issue:26 Volume:39 Page:7772-7780
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Uitdehaag Joost C. M.¹,van Alebeek Gert-Jan W. M.¹,van der Veen Bart A.¹,Dijkhuizen Lubbert¹,Dijkstra Bauke W.¹

Affiliation:

1. Center for Carbohydrate Bioengineering and Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands, and Center for Carbohydrate Bioengineering and Department of Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi000340x

Reference38 articles.

1. α-amylase family: Molecular biology and evolution

2. The concept of the α-amylase family: Structural similarity and common catalytic mechanism

3. Comparison of the domain-level organization of starch hydrolases and related enzymes

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