Physical Chemistry : An Indian Journal
ISSN (PRINT): 0974-7524

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Cyclodextrin Glycosyltransferase Peer-review Journals

Enzyme cyclodextrin glycosyltransferase is closely related to α-amylases but has the unique ability to produce cyclodextrins from starch. To characterize this specificity we determined a mutant cyclodextrin glycosyltransferase in complex with its product γ-cyclodextrin, which reveals for the first time how cyclodextrin is competently bound. Across subsites the cyclodextrin ring binds in a twisted mode similar to linear sugars, giving rise to deformation of its circular symmetry. At subsites −3 and +2, the cyclodextrin binds in a manner different from linear sugars. 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. On this basis, a role of the individual residues during the cyclization reaction cycle is proposed.

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Citations : 250

Physical Chemistry : An Indian Journal received 250 citations as per Google Scholar report

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