If an enzyme is bound by an allosteric effector what aspect of that enzyme is ch
ID: 71826 • Letter: I
Question
If an enzyme is bound by an allosteric effector what aspect of that enzyme is changed (select all that apply?
Question 9 options:
A) nothing
B) the tertiary structure of the enzyme
C) the shape of the active site
D) the shape of the substrate
E) the shape of the product
You have purified an enzyme found in a bacteria isolated in an acidic hot pool in Yellowstone National Park that catalyzes the addition of a phosphate to a ribose sugar. Which of the following is most likely to be true of this particular enzyme (choose one)?
Question 10 options:
this enzyme will function better at a high pH
this enzyme will function better at higher temperatures than room temperature
this enzyme is competitively regulated by other sugars
the primary structure of this enzyme is determined by its temperature
the enzyme will function best when it is denatured
A)this enzyme will function better at a high pH
B)this enzyme will function better at higher temperatures than room temperature
C)this enzyme is competitively regulated by other sugars
D)the primary structure of this enzyme is determined by its temperature
E)the enzyme will function best when it is denatured
Explanation / Answer
Answer 9. The allosteric effector will change the shape of the active site.
Explanation: Allosteric enzymes have regulatory subunits, either activators and inhibitors, collectively known as effectors. These effectors changes the shape of active site, Inhibitors causes the allosteric enzyme to get inactive shape and activators create the active shape.
Answer 10. This enzyme will function better at higher temperatures than room temperature.
Explanation. The enzyme obtained are thermophile or hyperthermophile which workks at optimum level at higher temepratures.
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