J
Joost C.M. Uitdehaag
Researcher at University of Groningen
Publications - 44
Citations - 3718
Joost C.M. Uitdehaag is an academic researcher from University of Groningen. The author has contributed to research in topics: Cyclodextrin glycosyltransferase & Cyclodextrin. The author has an hindex of 26, co-authored 43 publications receiving 3371 citations. Previous affiliations of Joost C.M. Uitdehaag include Schering-Plough & University of Oxford.
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Journal ArticleDOI
Properties and applications of starch-converting enzymes of the α-amylase family
Marc J. E. C. van der Maarel,Bart A. van der Veen,Joost C.M. Uitdehaag,Hans Leemhuis,Lubbert Dijkhuizen +4 more
TL;DR: The alpha-amylase family of glycosyl hydrolases as discussed by the authors is one of the most common types of enzymes used in industrial applications and has a (beta/alpha) 8-barrel structure with conserved amino acid residues.
Journal ArticleDOI
X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family.
Joost C.M. Uitdehaag,Renee Mosi,Kor H. Kalk,Bart A. van der Veen,Lubbert Dijkhuizen,Stephen G. Withers,Bauke W. Dijkstra +6 more
TL;DR: Two X-ray structures of CGTase complexes are determined, which give evidence for substrate distortion and the covalent character of the intermediate and for the first time show, in atomic detail, how catalysis in the α-amylase family proceeds by the concerted action of all active site residues.
Journal ArticleDOI
Engineering of cyclodextrin glycosyltransferase reaction and product specificity.
TL;DR: A particularly interesting enzyme is cyclodextrin glycosyltransferase (CGTase) as mentioned in this paper, which has the unique capability of forming cyclodesxtrins from starch.
Journal ArticleDOI
The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms
Bart A. van der Veen,Gert-Jan W. M. van Alebeek,Joost C.M. Uitdehaag,Bauke W. Dijkstra,Lubbert Dijkhuizen +4 more
TL;DR: The rate of interconversion of linear and circular conformations of oligosaccharides in the cyclization and coupling reactions was found to determine the reaction rate and will allow rational design of CGTase mutant enzymes synthesizing cyclodextrins of specific sizes.
Journal ArticleDOI
The Cyclization Mechanism of Cyclodextrin Glycosyltransferase (CGTase) as Revealed by a γ-Cyclodextrin-CGTase Complex at 1.8-Å Resolution
TL;DR: Sequence comparisons and site-directed mutagenesis experiments support the conclusion that subsites −3 and +2 confer the cyclization activity in addition to subsite −6 and Tyr-195, and a role of the individual residues during thecyclization reaction cycle is proposed.