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• W1551134780 abstract "Abstract Interactions of specific and nonspecific agents at the dihydroxyacetone-P and glyceraldehyde-3-P sites of rabbit muscle aldolase are shown by several methods: quenching of protein fluorescence, protection against the destructive action of trypsin, the inhibition of initial rates and of equilibrium exchange rates, and the inactivation caused by NaBH4. It is concluded from inactivation and labeling studies that glycolaldehyde-P can form a Schiff's base at the dihydroxyacetone-P site. d-Glyceraldehyde-3-P and erythrose-4-P, like dihydroxyacetone-P, cause fluorescence quenching at low concentration, whereas l-glyceraldehyde-3-P, which is a good acceptor for dihydroxyacetone-P, does not. The competitive inhibition shown by small anions such as Cl-, Pi, and ethyl-P is first order for these anions with fructose-1-P as the substrate but approximately second order with fructose-1,6-di-P as substrate. This suggests that binding of fructose-1-P to the enzyme is prevented by an anion bound to the dihydroxyacetone-P site, but not by one at the aldehyde-P site, whereas fructose-di-P binding is prevented by anion interaction with either site. Acetol-P ([see PDF for equation]) is a substrate for the proton exchange reaction of aldolase. It has a much higher Km than dihydroxyacetone-P, the maximum velocity of exchange is about 17% as great, and its rate of condensation with glyceraldehyde-3-P only about 1% that found with dihydroxyacetone-P. l-Glyceraldehyde-3-P is a competitive inhibitor of the proton exchange reaction of acetol-P but does not react with the dihydroxyacetone-P site as shown by lack of fluorescence quenching. This suggests that, although the enzyme can bind aldehyde, the complex is inappropriate for productive reaction with dihydroxyacetone-P. This is consistent with earlier studies requiring that the condensation is an ordered reaction with dihydroxyacetone-P reacting before aldehyde. The inactivation of aldolase as a result of reaction with l-glyceraldehyde-3-P is like that produced by carboxypeptidase in that it seems to inhibit the rate of —C—H bond cleavage and not —C—C bond cleavage of fructose-di-P. This is concluded since that transaldolase action of the treated enzyme with acetaldehyde as an acceptor is not much slower than that of untreated enzyme. The rate of inactivation with l-glyceraldehyde-3-P shows saturation kinetics with a Kinactivation that agrees with its Ki as a competitive inhibitor of fructose-1-P cleavage. However, in view of the finding that the transaldolase activity of the treated enzyme is unimpaired, the locus of this l-glyceraldehyde-3-P action cannot be that of the fructose-di-P binding. Those compounds that quench protein fluorescence also protect aldolase from inactivation by trypsin, whereas aldehydes such as dl-glyceraldehyde and l-glyceraldehyde-3-P form complexes that are more susceptible to trypsin action. Carboxypeptidase treatment of aldolase is observed to produce a large decrease in Km of fructose-di-P. This is contrary to the findings of others, but is required by theory if the ordered reaction mechanism is correct and if the effect of carboxypeptidase action is restricted to the step for protonation of the enzyme-dihydroxyacetone-P eneamine, as is believed." @default.
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• W1551134780 date "1969-01-01" @default.
• W1551134780 modified "2023-10-11" @default.
• W1551134780 title "Studies on the Interaction of Aldolase with Substrate Analogues" @default.
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• W1551134780 doi "https://doi.org/10.1016/s0021-9258(19)78201-5" @default.
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