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• W2316573842 endingPage "269" @default.
• W2316573842 startingPage "263" @default.
• W2316573842 abstract "Glycosyltransferases comprise a group of enzymes that catalyze the transfer of glycosyl residues from donors containing nucleoside phosphates to other molecules. The molecular details of the catalytic mechanism involving these enzymes are not well understood. Hybrid QM/MM methods have become important in providing new insights into the atomic details of enzymatic reactions. The QM/MM calculations of GnT-I and β4GalT-1 show that inverting glycosyltransferases utilize an SN2 type mechanism, with one amino acid functioning as a base catalyst. In addition, the computed transition state structures provide a rational basis for the design of transition state analog inhibitors. Keywords: Glycosyltransferases, catalytic mechanisms, QM(DFT)/MM methods, transition state structures, GnT-I, b4GalT-1, SN2 type mechanism" @default.
• W2316573842 created "2016-06-24" @default.
• W2316573842 creator A5006856491 @default.
• W2316573842 date "2011-08-01" @default.
• W2316573842 modified "2023-10-17" @default.
• W2316573842 title "QM/MM Insight on Enzymatic Reactions of Glycosyltransferases" @default.
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• W2316573842 doi "https://doi.org/10.2174/157019311796197490" @default.
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