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Results: 1-10 |
Results: 10
Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase
Authors: Uitdehaag, JCM van der Veen, BA Dijkhuizen, L Elber, R Dijkstra, BW
Citation: Jcm. Uitdehaag et al., Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase, PROTEINS, 43(3), 2001, pp. 327-335
Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase
Authors: van der Veen, BA Leemhuis, H Kralj, S Uitdehaag, JCM Dijkstra, BW Dijkhuizen, L
Citation: Ba. Van Der Veen et al., Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase, J BIOL CHEM, 276(48), 2001, pp. 44557-44562
Engineering of cyclodextrin glycosyltransferase reaction and product specificity
Authors: van der Veen, BA Uitdehaag, JCM Dijkstra, BW Dijkhuizen, L
Citation: Ba. Van Der Veen et al., Engineering of cyclodextrin glycosyltransferase reaction and product specificity, BBA-PROT ST, 1543(2), 2000, pp. 336-360
Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase alpha-cyclodextrin production
Authors: van der Veen, BA Uitdehaag, JCM Penninga, D van Alebeek, GJWM Smith, LM Dijkstra, BW Dijkhuizen, L
Citation: Ba. Van Der Veen et al., Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase alpha-cyclodextrin production, J MOL BIOL, 296(4), 2000, pp. 1027-1038
The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms
Authors: van der Veen, BA van Alebeek, GJWM Uitdehaag, JCM Dijkstra, BW Dijkhuizen, L
Citation: Ba. Van Der Veen et al., The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms, EUR J BIOCH, 267(3), 2000, pp. 658-665
The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 - Implications for product inhibition and product specificity
Authors: van der Veen, BA Uitdehaag, JCM Dijkstra, BW Dijkhuizen, L
Citation: Ba. Van Der Veen et al., The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 - Implications for product inhibition and product specificity, EUR J BIOCH, 267(12), 2000, pp. 3432-3441
Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity
Authors: Uitdehaag, JCM van Alebeek, GJWM van der Veen, BA Dijkhuizen, L Dijkstra, BW
Citation: Jcm. Uitdehaag et al., Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity, BIOCHEM, 39(26), 2000, pp. 7772-7780
X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family
Authors: Uitdehaag, JCM Mosi, R Kalk, KH van der Veen, BA Dijkhuizen, L Withers, SG Dijkstra, BW
Citation: Jcm. Uitdehaag et al., X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family, NAT ST BIOL, 6(5), 1999, pp. 432-436
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-angstrom resolution
Authors: Uitdehaag, JCM Kalk, KH van der Veen, BA Dijkhuizen, L Dijkstra, BW
Citation: Jcm. Uitdehaag et al., The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-angstrom resolution, J BIOL CHEM, 274(49), 1999, pp. 34868-34876
Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase
Authors: Mosi, R Sham, H Uitdehaag, JCM Ruiterkamp, R Dijkstra, BW Withers, SG
Citation: R. Mosi et al., Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase, BIOCHEM, 37(49), 1998, pp. 17192-17198
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