Contribution of W229 to the transglycosylation activity of 4-α-glucanotransferase from Pyrococcus furiosus

Cited 29 time in scopus
Metadata Downloads
Title
Contribution of W229 to the transglycosylation activity of 4-α-glucanotransferase from Pyrococcus furiosus
Author(s)
S Y Tang; S J Yang; H Cha; Eui-Jeon Woo; C Park; K H Park
Bibliographic Citation
Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1764, no. 10, pp. 1633-1638
Publication Year
2006
Abstract
A W229H mutant of 4-α-glucanotransferase (4-α-GTase) from Pyrococcus furiosus was constructed and its catalytic properties were studied to investigate the role of W229 in the catalytic specificities of the enzyme. Various activities and kinetic parameters were determined for the wild-type and W229H mutant enzymes. The transglycosylation factor and transglycosylation activity of the mutant enzyme markedly decreased, but its hydrolysis activity was scarcely affected. It was discovered that the kcat/Km value of transglycosylation activity significantly decreased to about 15% of that of the wild type, while kcat/Km value of hydrolysis activity changed little for the mutant enzyme. The hydrophobicity of W229 was thought to be critical to the transglycosylation activity of the enzyme based on the enzyme's modeled tertiary structures.
Keyword
4-α-glucanotransferase (4-α-GTase)hydrolysis activityhydrophobicitysite-directed mutagenesistransglycosylation activity
ISSN
1570-9639
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbapap.2006.08.013
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.