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  • Title: Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge.
    Author: Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L.
    Journal: Proteins; 2004 Jan 01; 54(1):128-34. PubMed ID: 14705029.
    Abstract:
    Cyclodextrin glycosyltransferase (CGTase) catalyzes the formation of cyclodextrins from starch. Among the CGTases with known three-dimensional structure, Thermoanaerobacterium thermosulfurigenes CGTase has the highest thermostability. By replacing amino acid residues in the B-domain of Bacillus circulans CGTase with those from T. thermosulfurigenes CGTase, we identified a B. circulans CGTase mutant (with N188D and K192R mutations), with a strongly increased activity half-life at 60 degrees C. Asp188 and Arg192 form a salt bridge in T. thermosulfurigenes CGTase. Structural analysis of the B. circulans CGTase mutant revealed that this salt bridge is also formed in the mutant. Thus, the activity half-life of this enzyme can be enhanced by rational protein engineering.
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