Explain Fig. 8.13 in your own words. Be sure to highlight ALL starred portions discussed in class.
Describe the main idea of the first paragraph on p.155 on the topic of how substrate concentration affects reaction rate when an enzyme is present.
The name of the enzyme shown in the very first diagram in 8.4 is ____________________. (the diagram showing the hydrolysis of sucrose).
The reaction profiled in Fig. 8.12 must be an ___________________ reaction since it has a negative deltaG.
Molecule C-D is a reactant of the reaction shown in Fig. 8.12.
_________________________ is the energy needed to start a reaction.
The size of the activation energy will determine the rate of a reaction since it determines how much energy investment is needed for the reaction to proceed.
Enzymes cannot change the deltaG of a reaction - they can only speed a reaction that would occur anyway.
Enzymes are extremely specific to their ________________ because of their precise 3-D (tertiary) shapes. Even very similar molecules will not fit into an enzyme's active site.
Check any of the following that WOULD change if a reaction proceeded with vs. without an enzyme.
DeltaG (free energy change)
Rate of reaction
The _____________________ is the precise place on an enzyme that a substrate will bind.
Every enzyme has an _________________ temperature and pH at which its 3D shape is most perfect and therefore at which it works best.
Check any of the following that are disrupted if the temperature of a reaction gets TOO hot.
Van der waals interactions
Initially, raising the temperature of an enzyme-catalyzed reaction slightly will speed the reaction rate because it causes more _______________ between enzymes and substrates as the molecules move around more.
See Fig. 8.16 A. The difference between the optimal temperature of a typical human enzyme and that of a thermophilic bacteria is ________ degrees Celcius.
See Fig. 8.16 B. Pepsin works best at basic pHs and trypsin works best at acidic pHs.
_______________________, like vitamins, can bind to enzymes and help them to work.
An ___________________ would be like the opposite of a cofactor since it would bind to an enzyme and DECREASE its ability to function.
____________________ inhibitors bind in the active site of the enzyme and therefore prevent the substrate from binding.
_____________________ inhibitors don't bind in the active site - they bind to another place on the enzyme that causes its 3D shape to change and therefore prevents the substrate from binding.
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