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Glycosyl-enzyme intermediates direct observation

The canonical mechanism shown in Figure 5.32 requires the same carboxylate group which acts as a general acid in the first step to act as a general base in the second. Its pAa must, therefore, decrease between the free enzyme and the glycosyl-enzyme intermediate. Direct NMR observation of active site carboxy-lates in the GH 11 p-xylanase of B. circulans already discussed in Section 5.4.2 indicated that the acid-base catalytic Glu 172 had a (microscopic) pAa of 6.7 in the free enzyme and 4.2 in the 2-deoxy-2-fluoro-a-xylobiosyl enzyme generated from the Withers inactivator 2,4-dinitrophenyl 2 -deoxy-2 -fluoro-p-xylobioside. ... [Pg.387]

See other pages where Glycosyl-enzyme intermediates direct observation is mentioned: [Pg.380]    [Pg.382]    [Pg.2337]    [Pg.442]    [Pg.278]    [Pg.340]    [Pg.295]   


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Direct glycosylation

Direct observation

Directed enzymes

Glycosyl enzyme intermediates

Intermediates, direct observation

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