Characterization of a novel debranching enzyme from Nostoc punctiforme possessing a high specificity for long branched chains = Nostoc punctiforme로 부터 얻은 신규 탈가지화 효소의 특성

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Title
Characterization of a novel debranching enzyme from Nostoc punctiforme possessing a high specificity for long branched chains = Nostoc punctiforme로 부터 얻은 신규 탈가지화 효소의 특성
Author(s)
J H Choi; H Lee; Y W Kim; J T Park; Eui-Jeon Woo; M J Kim; B H Lee; K H Park
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 378, no. 2, pp. 224-229
Publication Year
2009
Abstract
A novel debranching enzyme from Nostoc punctiforme PCC73102 (NPDE) exhibits hydrolysis activity toward both α-(1,6)- and α-(1,4)-glucosidic linkages. The action patterns of NPDE revealed that branched chains are released first, and the resulting maltooligosaccharides are then hydrolyzed. Analysis of the reaction with maltooligosaccharide substrates labeled with 14C-glucose at the reducing end shows that NPDE specifically liberates glucose from the reducing end. Kinetic analyses showed that the hydrolytic activity of NPDE is greatly affected by the length of the substrate. The catalytic efficiency of NPDE increased considerably upon using substrates that can occupy at least eight glycone subsites such as maltononaose and maltooctaosyl-α-(1,6)-β-cyclodextrin. These results imply that NPDE has a unique subsite structure consisting of -8 to +1 subsites. Given its unique subsite structure, side chains shorter than maltooctaose in amylopectin were resistant to hydrolysis by NPDE, and the population of longer side chains was reduced.
Keyword
Substrate specificityBranched cyclodextrinDebranching enzymeNostoc punctiformeSubsite structure
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2008.11.020
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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