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Standard free energy doesn't change with an enzyme. Rather, the enzyme acts to redirect that reaction in a particular way, lowering the required energy for the reaction to occur but not changing the energy amount involved.
Well, unlike competitive inhibitors the non-competitive inhibitors will not compete the active site of the enzyme with substrate . Instead, it will combine with the enzyme somewhere except the ative site and alter the whole shape of the enzymes therefore the active site of substrate and enzyme are not the same and therefore no enzyme-substrate complex can be formed and the enzymatic effect can't be restored becausr the enzymes are now denatured
Fractional crystalization of Hydrogen Peroxide would involve lowering the temperature of the solution to just above the melting point. This will depend on the concentration and it is NOT linear. For instance, a 3% solution as is found in most drugstores will freeze at about -2C, 30% at about -25C, 35% at -33C, 50% at -52C, 70% at -40C and finally 90% at about -11C.
actors such as temperature and pH can affect an enzyme's rate of reaction because enzymes are sensitive to pH and heat. Most enzymes can only function in a particular temperature or pH range, and as the enzyme works out of its normal temperature and pH range, it will denature (change in shape so that the active site no longer fits with the substrate and the enzyme can't function).
Some examples of a non-electrolyte solution in water would be a solution of sugar, or a solution of urea. These do no ionize in solution and so are non-electrolytes.
It would lower the speed of the reaction but will do no harm to the enzyme.
Standard free energy doesn't change with an enzyme. Rather, the enzyme acts to redirect that reaction in a particular way, lowering the required energy for the reaction to occur but not changing the energy amount involved.
by lowering the activation energy of reactions
Lowering prices so that they can compete with their competitors would be my guess
The allosteric site is distinct from the active site, and does not affect the substrate specificity of the enzyme
Lowering the body temperature would lower the temperature in the cells, this causes the substrates to slow down, in a sense be less hyperactive, thus lowering the chance that the substrate will come in contact with its given enzyme. This will lower the overall Cellular Metabolism
Non-working enzyme → no ATP → no energy → death.
Just like always, deviating from the desired normal functioning for the enzyme, whether it be in temperature or pH, would result in the enzyme denaturing and therefore being unable to for enzyme substrate complexes, therefore reducing the overall reaction rate.
(2) increase, then decrease
enzyme catalyze the biochemical reactions by lowering their activation energy. An enzyme which take part in such reaction wont be lost or gained any chemical structure and it would be the same after the reaction.
Yes, it would effect the enzyme as i would become acidic. If it becomes too acidic then the shape of the active site will change and the substrate will no longer fit and therefore no reaction can take place. A low pH will denature the enzyme ( cause the protein structure to change shape)