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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
- Files in This Item:
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