Journal
FEBS LETTERS
Volume 514, Issue 2-3, Pages 189-192Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02362-1
Keywords
cyclodextrin glycosyltransferase; transglycosylation; transglycosidase; enhanced hydrolysis; acceptor subsite
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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 Thermoanacrobacterium 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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