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Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase

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Title: Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase
Authors: Saburi, Wataru Browse this author →KAKEN DB
Rachi-Otsuka, Hiroaki Browse this author
Hondoh, Hironori Browse this author
Okuyama, Masayuki Browse this author →KAKEN DB
Mori, Haruhide Browse this author →KAKEN DB
Kimura, Atsuo Browse this author →KAKEN DB
Keywords: Dextran glucosidase
alpha-Glucosidase
Oligo-1,6-glucosidase
Substrate specificity
Glycoside hydrolase family 13
Issue Date: 25-Mar-2015
Publisher: Elsevier
Journal Title: Febs letters
Volume: 589
Issue: 7
Start Page: 865
End Page: 869
Publisher DOI: 10.1016/j.febslet.2015.02.023
PMID: 25728274
Abstract: Glycoside hydrolase family 13 contains exo-glucosidases specific for alpha-(1 -> 4)- and alpha-(1 -> 6)-linkages including alpha-glucosidase, oligo-1,6-glucosidase, and dextran glucosidase. The alpha-(1 -> 6)-linkage selectivity of Streptococcus mutans dextran glucosidase was altered to alpha-(1 -> 4)-linkage selectivity through site-directed mutations at Val195, Lys275, and Glu371. V195A showed 1300-fold higher k(cat)/K-m for maltose than wild-type, but its k(cat)/K-m for isomaltose remained 2-fold higher than for maltose. K275A and E371A combined with V195A mutation only decreased isomaltase activity. V195A/K275A, V195A/E371A, and V195A/K275A/E371A showed 27-, 26-, and 73-fold higher k(cat)/K-m for maltose than for isomaltose, respectively. Consequently, the three residues are structural elements for recognition of the alpha-(1 -> 6)-glucosidic linkage. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Type: article (author version)
URI: http://hdl.handle.net/2115/60921
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 木村 淳夫

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