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Title 

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

Authors 

S H ParkH K KangJ H ShimEui-jeon WooJ S HongJ W KimB H OhB H LeeH ChaK H Park

Publisher 

Japan Society for Bioscience, Biotechnology and Agrochemistry

Issue Date 

2007

Citation 

Bioscience Biotechnology and Biochemistry, vol. 71, no. 6, pp. 1564-1567

Keywords 

amylopectinamylosecyclodextrin-degrading enzymemutagenesisthermus sp. maltogenic amylase (ThMA)amino acidscatalyst activitydimerssubstitution reactionsamylase

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.

ISSN 

0916-8451

Link 

http://dx.doi.org/10.1271/bbb.70017

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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