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Glucose activated, reactions

During normal activity, a person uses the equivalent of about 10 MJ of energy a day. Assume that this value represents AG, and estimate the average current through your body in the course of a day, assuming that all the energy that we use arises from the reduction of 02 in the glucose oxidation reaction. See Box 12.1. [Pg.645]

When (1) and (2) are coupled in a reaction catalyzed by hexokinase, phosphorylation of glucose readily proceeds in a highly exergonic reaction that under physiologic conditions is irreversible. Many activation reactions follow this pattern. [Pg.84]

Figure 4. Catalytic activity of the Au/C large-scale preparations and the 2g preparation in glucose oxidation. Reaction conditions glucose 50wt.% S/M ratio 20,000 O2 flow INL/min stirring rate 1700rpm. pH 9.5. Figure 4. Catalytic activity of the Au/C large-scale preparations and the 2g preparation in glucose oxidation. Reaction conditions glucose 50wt.% S/M ratio 20,000 O2 flow INL/min stirring rate 1700rpm. pH 9.5.
R6. Ramot, B., Ashkenazi, I., Rimon, A., Adam, A., and Sheba, C., Activation of glucose-6-phosphate dehydrogenase of enzyme deficient subjects 2. Properties of the activator and the activation reaction. J. Clin. Invest. 40, 611-616 (1961). [Pg.305]

Kohen, A., Jonsson, T. and Klinman, J.P. (1997). Effects of protein glycosylation on catalysis changes in hydrogen tunnehng and enthalpy of activation in the glucose oxidase reaction. Biochemistry 36, 2603-2611... [Pg.78]

The enzymatic activity versus pH is thus generally a bell-shaped curve as in Fig. 6. An autocatalytic effect may appear when the reaction products have an acid-base effect (often the case). A simple example is the glucose oxidase reaction, shown in Fig. 7. Notably, the rate versus product (H+) curve indicates an autocatalytic effect on the alkaline branch, that is, for pH>pH (see Fig. 6). Systems presenting analogous properties have been studied by R. Caplan et al.27 and we also learn more about them from D. Thomas in this volume. [Pg.6]

How a preferential binding of a reactant species over a product species affects the thermodynamic activities is influenced by the nature of the reaction. For reactions that occur on the surface of the enzyme, the preferential binding of reactant species causes its activity to be increased relative to that of the product and the conversion to products on the binding surface is favored. When the reaction takes place in the bulk solution, a preferential binding of the reactant species to the surface lowers its activity relative to that of the product, and the reverse reaction becomes favored. The hexakinase-glucose-ATP reaction is an example of the first type. [Pg.219]

Group-transfer reactions play a variety of roles. Reaction 5 is representative of such a reaction. A phosphoryl group is transferred from the activated phosphoryl-group carrier, ATP, to glucose. This reaction traps glucose in the cell so that further catabolism can take place. [Pg.584]

It is instructive to consider how structural aspects of the enzyme-substrate binding produce thermodynamic conditions that drive the reaction to completion. As we have noted, the ArG° for the glucose phosphorylation reaction (16.5) is quite positive, and the relative activities (concentrations) of the reactant ( g) and product ( g6p) glucose species needed to make ArG negative are not observed physiologically. However, the activities of the phosphate ion (ap,) and water (oh2o) also enter into the determination of the actual ArG as given by the equation... [Pg.218]

Thus, the n-pentenyl glycoside 51 (Scheme 12a) reacted in the presence of methanol to give the methyl glycoside 52. An even more exciting development is shown in Scheme 12b where the "alcohol" is diacetone glucose. The reaction 51 —> 53 allows the direct formation of the disaccharide from the activated glycoside. [Pg.101]

The mechanism of the entry of fructose into the Maillard reaction (a series of sugar/amino acid processes in vivo) has been studied by DFT the order of reactivity for the isomers is predicted as a- > /3- > open-chain. Heyns rearrangement products are most favourable under basic conditions, possible under neutral conditions, but unfeasible at or below glycine s isoelectric point. Kinetic and activation parameters have been reported for the corresponding glucose/proline reaction. ... [Pg.4]

Epinephrine is a hormone that causes extremely rapid responses. One of the responses to this hormone is an increased liberation of liver glycogen as glucose. This reaction has been found to be limited by the enzyme phosphorylase. Liver phosphorylase exists as the active enzyme and as the inactive, dephosphophosphorylase. Epinephrine, and also the hyperglycemic factor, glucagon, have been found to stimulate the formation of active phosphorylase. This stimulation is mediated by an adenine nucleotide liberated from cell particles by an action of the hormones. The liberation of the nucleotide has been demonstrated in cell-free systems. The nucleotide in an unexplained manner, perhaps indirectly or after metabolic conversion to another form, alters the activity of either the kinase or the phosphatase so that the steady-state concentration of active phosphorylase is increased, i ... [Pg.396]


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See also in sourсe #XX -- [ Pg.301 , Pg.302 ]




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