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EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.13quantum mechanics/molecular mechanics study on mechanism. Residue D665 acts as an acid to protonate the glycoside oxygen, which is concerted with the cleavage of the glycoside bond. Residue D553 functions as the nucleophile to attack the anomeric carbon to form the glycosyl-enzyme intermediate. The glycosylation process follows a stepwise mechanism. The deprotonated residue D553 further acts as a catalytic base to abstract the C2-proton of the glucosyl residue. The proton abstraction in the deglycosylation/elimination step is calculated to be the rate-limiting step of the whole catalytic reaction 749283
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.13structure contains a (beta/alpha)8-barrel catalytic domain with B and B' subdomains, an N-terminal domain N, and the C-terminal domains C and D. The N-terminal domain binds a trisaccharide. Complexes of the enzyme with acarbose and 1-dexoynojirimycin and two different covalent glycosyl-enzyme intermediates show that the aspartic acid residues Asp553 and Asp665 are the catalytic nucleophile and acid, respectively. The catalytic nucleophile is in a position to act also as a base that abstracts a proton from the C2 carbon atom of the covalently bound subsite -1 glucosyl residue 730019
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