Conformational adaptability of the active site of beta-galactosidase. Interaction of the enzyme with some substrate analogous effectors.
The action of different effectors, glycosides, and alcohols on the reactions catalyzed by beta-galactosidase is analyzed in this paper. Effectors as large as tri- and tetrasaccharides have no effect on the enzyme activity, suggesting that the binding site has rather small size. Most of the beta-galactosides produce a competitive inhibition. The other compounds assayed behave either as noncompetitive inhibitors, and they are deadened inhibitors, or as uncompetitive inhibitors which exhibit a better affinity for the chemical intermediate than for free enzyme; nearly all of them give transfer products. The analysis of the data indicates that the active center of beta-galactosidase is made up of two subsites: a galactose and a glucose subsite. This latter site is in a more favorable conformation in the galactosylenzyme than in free enzyme; possibly it might even by generated by the galactose binding. Conformational rearrangements of the active center deduced from the inhibition data have been directly observed by differential spectroscopy. The conformational adaptability of the enzyme and its consequence for the functional properties of beta-galactosidase are discussed.
D001665:Binding Sites; D005696:Galactosidases / Q000378:metabolism*; D007700:Kinetics; D011487:Protein Conformation; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005696:Galactosidases; D001616:beta-Galactosidase