The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping‐Pong mechanism
Open Access
- 3 January 1994
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 337 (1), 66-70
- https://doi.org/10.1016/0014-5793(94)80631-4
Abstract
A new photometric assay of the disproportionation activity of cyclodextrin glucanotransferase (CGTase) using 3‐ketobutylidene‐β‐2‐chloro‐4‐nitrophenyl ‐maltopentaoside as the donor, proved that the transglycosylation reaction of CGTase was operated by a Ping‐Pong Bi Bi mechanism. The values of the k cat/K m acceptor proved that the same configurations of free hydroxyl groups with those of d‐glucopyranose at C2, C3 and C4 positions were required for the acceptors used by CGTase. The structure around C6 on acceptors was not essential for acceptor function, but it was recognized by CGTase, since the values of k cat/K m for d‐xylose were smaller than that for d‐glucose. The value of k cat/K mfor maltose was about 20‐times larger than that for d‐glucose, indicating that at least two glucopyranosyl rings are recognized by the acceptor binding sites.Keywords
This publication has 26 references indexed in Scilit:
- Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of the replacement on pH dependence and transition-state stabilizationBiochemistry, 1993
- Catalytic center of cyclodextrin glycosyltransferase derived from x-ray structure analysis combined with site-directed mutagenesisBiochemistry, 1992
- Site-directed mutagenesis of active site residues in Bacillus subtilis α-amylaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α‐amylases Site‐directed mutagenesis of the conserved two Asp and one Glu residuesFEBS Letters, 1992
- An increase in the transglycosylation activity of Saccharomycopsis α-amylase altered by site-directed mutagenesisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolutionJournal of Molecular Biology, 1991
- Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from AspergillusBiochemistry, 1990
- Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylaseProtein Engineering, Design and Selection, 1990
- Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutationBiochemistry, 1983
- Acceptor specificity of the transglycosylation catalyzed by cyclodextrin glycosyltransferase.Agricultural and Biological Chemistry, 1978