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Ground-state analog enzyme

The chemical interest of these trace amount proteins stems from the fact that they can be used as catalysts or enzyme analogs for almost any chemical reaction (Tramontano et al., 1986 Pollack et al., 1986 Lemer et al., 1991). The fundamental difference between antibodies and enzymes does not relate so much to the protein structures as to the structure and lifetime of the substrates. Antibodies selectively bind molecules in their ground state, whereas enzymes selectively produce and then bind more strongly to short-lived transition states. Antibody-antigen complexes tend toward precipitation, whereas enzyme-transition state complexes react to enzyme-product complexes, which immediately dissociate. In both cases, however, the same noncovalent bonds are used. [Pg.520]

This analysis reveals that enzymes bind the transition state more tightly than the ground state by a factor approximately equal to the rate of acceleration (ie, Kjs/Ks kuncaJkcat)- This method has been used to show, for example, that the peptide phos-phonate inhibitors of carboxypeptidase A are true transition state analogs. [Pg.359]

R. H. Abeles, Enzyme Inhibitors Ground State/ Transition-State Analogs , Drug, Dev. Res. 1987, 10, 221-234. [Pg.367]

The aqueous cores of reverse micelles are of particular interest because of their analogy with the water pockets in bioaggregates and the active sites of enzymes. Moreover, enzymes solubilized in reverse micelles can exhibit an enhanced catalytic efficiency. Figure B4.3.1 shows a reverse micelle of bis(2-ethylhexyl)sulfosuccinate (AOT) in heptane with three naphthalenic fluorescent probes whose excited-state pK values are much lower than the ground-state pK (see Table 4.4) 2-naphthol (NOH), sodium 2-naphthol sulfonate (NSOH), potassium 2-naphthol-6,8-disulfonate (NSOH). The spectra and the rate constants for deprotonation and back-recombination (determined by time-resolved experiments) provide information on the location of the probes and the corresponding ability of their microenvironment to accept a proton , (i) NDSOH is located around the center of the water pool, and at water contents w = [H20]/[A0T] >... [Pg.107]

In our context, an important class of reversible inhibitors are the transition state analogs [18], which are stable compounds designed to mimic the structure of an intermediate in the path of substrate s transformation by the enzyme. Such analogs are based in Pauling s postulate [19], which states that "an enzyme recognises and binds more tightly to the transition state than to the ground state of the substrate". [Pg.301]


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Analog ground

Analogous enzymes

Enzyme analogs

Ground-state analog

Ground-state analog enzyme inhibitors

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