상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

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

Authors 

J H ChoiH LeeY W KimJ T ParkEui-Jeon WooM J KimB H LeeK H Park

Publisher 

Elsevier

Issue Date 

2009

Citation 

Biochemical and Biophysical Research Communications, vol. 378, no. 2, pp. 224-229

Keywords 

branched cyclodextrindebranching enzymenostoc punctiformesubsite structuresubstrate specificityalpha 1,4 glucosidealpha 1,6 glucosideamylopectinenzyme specificitybacterial enzyme

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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2008.11.020

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)