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Title 

Introducing transglycosylation activity in Bacillus licheniformis alpha-amylase by replacement of His235 with Glu

Authors 

P L TranH J ChaJ S LeeS H ParkEui-jeon WooK H Park

Publisher 

Elsevier

Issue Date 

2014

Citation 

Biochemical and Biophysical Research Communications, vol. 451, no. 4, pp. 541-547

Keywords 

Bacillus licheniformis thermostableBinding-subsite mappingSite-directed mutagenesisSubstrate transglycosylationTransfer productα-amylase

Abstract 

To understand the role of His and Glu in the catalytic activity of Bacillus licheniformis α-amylase (BLA), His235 was replaced with Glu. The mutant enzyme, H235E, was characterized in terms of its mode of action using labeled and unlabeled maltooctaose (Glc8). H235E predominantly produced maltotridecaose (Glc13) from Glc8, exhibiting high substrate transglycosylation activity, with Km = 0.38 mM and kcat/Km = 20.58 mM-1 s-1 for hydrolysis, and Km2 = 18.38 mM and kcat2/Km2 = 2.57 mM-1 s-1 for transglycosylation, while the wild-type BLA exhibited high hydrolysis activity exclusively. Glu235 - located on a wide open groove near subsite +1 - is likely involved in transglycosylation via formation of an α-1,4-glycosidic linkage and may recognize and stabilize the non-reducing end glucose of the acceptor molecule.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2014.08.019

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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