X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases.

@article{Strokopytov1995XraySO,
  title={X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases.},
  author={Boris Strokopytov and Dirk Penninga and H J Rozeboom and Kor H. Kalk and Lubbert Dijkhuizen and Bauke W Dijkstra},
  journal={Biochemistry},
  year={1995},
  volume={34 7},
  pages={2234-40}
}
Crystals of cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans strain 251 were soaked in buffer solutions containing the pseudotetrasaccharide acarbose, a strong amylase- and CGTase inhibitor. The X-ray structure of the complex was elucidated at 2.5-A resolution with a final crystallographic R value of 15.8% for all data between 8.0 and 2.5 A. Acarbose is bound near the catalytic residues Asp229, Glu257, and Asp328. The carboxylic group of Glu257 is at hydrogen bonding distance… CONTINUE READING
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