Modulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer

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Title
Modulation of substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer
Author(s)
S H Park; H K Kang; J H Shim; Eui-jeon Woo; J S Hong; J W Kim; B H Oh; B H Lee; H Cha; K H Park
Bibliographic Citation
Bioscience Biotechnology and Biochemistry, vol. 71, no. 6, pp. 1564-1567
Publication Year
2007
Abstract
To elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The kcat/Km value of the mutant for amylose increased significantly, whereas that for amylopectin decreased as compared to that of the wild-type enzyme. Thus, the substituted bulky amino acid residues modified the shape of the catalytic site, such that the ability of the enzyme to distinguish between small and large molecules like amylose and amylopectin was enhanced.
Keyword
AmyloseCyclodextrin-degrading enzymeMutagenesisAmylopectinThermus sp. Maltogenic amylase (ThMA)
ISSN
0916-8451
Publisher
T&F (Taylor & Francis)
DOI
http://dx.doi.org/10.1271/bbb.70017
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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