GROSS, M and AUERBACH, G and JAENICKE, R (1993) THE CATALYTIC ACTIVITIES OF MONOMERIC ENZYMES SHOW COMPLEX PRESSURE-DEPENDENCE. FEBS LETTERS, 321 (2-3). pp. 256-260. ISSN 0014-5793,
Full text not available from this repository.Abstract
High hydrostatic pressures in the biologically relevant range (less-than-or-equal-to 1,200 bar) are known to cause dissociation of oligomeric enzymes in vitro, whereas protein denaturation requires pressures far beyond this range. Pressure-induced inactivation phenomena attributable to neither of these effects are shown to occur in monomeric enzymes. Three different types of pressure dependence can be distinguished: (1) a linear dependence of catalytic rate constants on pressure, as predicted by the activated complex theory, observed for lysozyme and thermolysin; (2) a biphasic profile consisting of two linear contributions, found for trypsin; (3) maximum curves, as observed for both directions of the octopine dehydrogenase reaction. The third case may be ascribed to a pressure-induced decrease in the partial specific volume of the protein, resulting in reduced flexibility of the active site. This mechanism may also apply to the pressure-induced inactivation of assembly systems stabilized against dissociation in the cell.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEINS; DEHYDROGENASE; ACTIVATION VOLUME; COMPRESSIBILITY; HEN EGG-WHITE LYSOZYME; OCTOPINE DEHYDROGENASE; THERMOLYSIN; TRYPSIN |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54001 |
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