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  • Title: Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.
    Author: Leemhuis H, Dijkstra BW, Dijkhuizen L.
    Journal: FEBS Lett; 2002 Mar 13; 514(2-3):189-92. PubMed ID: 11943149.
    Abstract:
    Cyclodextrin glycosyltransferase (CGTase) efficiently catalyzes transglycosylation of oligo-maltodextrins, although the enzyme also has a low hydrolytic activity. Its +2 substrate binding subsite, which contains the conserved Phe184 and Phe260 residues, has been shown to be important for this transglycosylation activity [Nakamura et al. (1994) Biochemistry 33, 9929-9936]. Here we show that the amino acid side chain at position 260 also controls the hydrolytic activity of CGTase. Three Phe260 mutants of Thermoanaerobacterium thermosulfurigenes CGTase were obtained with a higher hydrolytic activity than ever observed before for a CGTase. These Phe260 mutations even changed CGTase from a transglycosylase into a starch hydrolase.
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