Volume changes during enzyme reactions. The influence of pressure on the action of invertase, dextranase and dextransucrase.
The pressure dependence of the maximum velocities and the Michaelis constants for the enzymes invertase and dextranase was measured up to 1400 bar. The corresponding activation volumes deltaV not equal to c and deltaV not equal to Km proved to be independent of pressure. Together with data from other sources the meaning of deltaV not equal to c and deltaV not equal to Km is established and the volume profiles of the reactions are constructed. These profiles are similar in contour to the volume profile of the dextran formation catalyzed by the enzyme dextransucrase, but the amount of the volume changes is very much larger for dextransucrase. The evaluation of salt effects shows, that for all three enzymes solvent interactions are not important in explaining the results. The reaction mechanisms seem to be governed by conformation changes of the enzymes. The larger effects in dextransucrase are explained by the produced dextran chain remaining tightly bound to the enzyme and being transported relative to the enzymes position in each reaction cycle.
D003910:Dextranase / Q000378:metabolism*; D003911:Dextrans; D005964:Glucosyltransferases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006874:Hydrostatic Pressure; D007700:Kinetics; D009994:Osmolar Concentration; D011487:Protein Conformation; D012997:Solvents; D013329:Structure-Activity Relationship; D013393:Sucrase / Q000378:metabolism*; D013395:Sucrose; D013816:Thermodynamics
D003911:Dextrans; D012997:Solvents; D013395:Sucrose; D005964:Glucosyltransferases; C020025:dextransucrase; D003910:Dextranase; D013393:Sucrase