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Retaining glycosidases kinetics

Scheme 5.2 Minimal kinetic scheme for a retaining glycosidase. The double displacement reaction involves two enzyme-substrate complexes, the second of which is commonly (but not always) a glycosylated enzyme. Scheme 5.2 Minimal kinetic scheme for a retaining glycosidase. The double displacement reaction involves two enzyme-substrate complexes, the second of which is commonly (but not always) a glycosylated enzyme.
The minimal kinetic scheme for a retaining glycosidase is given in Scheme 5.2. This scheme gives rise to expressions for kcat, and as shown in eqns... [Pg.307]

Figure 5.38 Burst kinetics showing liberation of aglycone during the establishment of a steady state during hydrolysis of a snbstrate by a retaining glycosidase, when the hydrolysis of the glycosyl-enzyme is rate determining. The glycone was fluorinated, so the experiment was performed in a conventional spectrometer (note time-scale). Note the burst of 0.03 absorbance units. Figure 5.38 Burst kinetics showing liberation of aglycone during the establishment of a steady state during hydrolysis of a snbstrate by a retaining glycosidase, when the hydrolysis of the glycosyl-enzyme is rate determining. The glycone was fluorinated, so the experiment was performed in a conventional spectrometer (note time-scale). Note the burst of 0.03 absorbance units.
A direct comparison of the kinetic data for the E217Q mutant with those reported for other acid/base mutants of retaining P-glycosidases is difficult, due... [Pg.219]


See other pages where Retaining glycosidases kinetics is mentioned: [Pg.117]    [Pg.360]    [Pg.195]    [Pg.492]    [Pg.298]    [Pg.302]    [Pg.313]    [Pg.253]    [Pg.372]    [Pg.401]    [Pg.634]    [Pg.8]    [Pg.395]    [Pg.397]    [Pg.405]    [Pg.407]    [Pg.253]    [Pg.548]    [Pg.209]    [Pg.326]    [Pg.3]    [Pg.143]    [Pg.404]    [Pg.3]    [Pg.412]    [Pg.266]    [Pg.200]    [Pg.995]    [Pg.545]    [Pg.979]   
See also in sourсe #XX -- [ Pg.383 ]




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