Bart A. van der Veen

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.

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.

TL;DR: Purified mutant CGTases were characterized with respect to raw starch binding and cyclization reaction kinetics on both soluble and raw starch, and it is shown that maltose binding site 1 is most important for raw starchbinding, whereas maltosebinding site 2 is involved in guiding linear starch chains into the active site.

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.

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.