[Possible role of the macromolecular environment in enzyme functioning in the cell. Interaction of E. coli beta-galactosidase with endogenous polycationic proteins and kinetic parameters of the enzyme in situ].
The effect of endogenous protein polycations on the kinetic properties of beta-galactosidase was studied. The dependence of kinetic properties of the enzyme (Km and V) in situ at the growth stage of microbial cultures was demonstrated. The observed phenomenon may be explained by the enzyme interaction with endogenous polycations. This interaction is of limited specificity, since it involves different types of biomolecules which display similar polyelectrolyte properties.
D001426:Bacterial Proteins / Q000378:metabolism*; D002412:Cations; D004926:Escherichia coli / Q000201:enzymology*; D005696:Galactosidases / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008954:Models, Biological; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D001426:Bacterial Proteins; D002412:Cations; D046911:Macromolecular Substances; D005696:Galactosidases; D001616:beta-Galactosidase
Vozmozhnaia rol' makromolekuliarnogo okruzheniia fermentov v ikh funktsionirovanii v kletke. Vzaimodeĭstvie beta-galaktozidazy E. coli s éndogennymi polikationnymi belkami i issledovanie kineticheskikh parametrov fermenta in situ.