When a molecule similar to the correct substrate interacts with ...

[Diane]

When a molecule similar to the correct substrate interacts with the active site of an enzyme, the process is called
 
  A) competitive inhibition.
  B) noncompetitive inhibition.
  C) irreversible inhibition.
  D) activation.
  E) covalent modification.

Question 2

1.06g of Na2CO3 is dissolved in 100mL of water. What is the molarity of Na+ ions in the solution?
 
  A) 0.2 M
  B) 0.1 M
  C) 1  10-4 M
  D) 0.01 M

Question 3

What is the most likely charge on an ion formed by an element with a valence electron configuration of ns2np1?
 
  A) 3-
  B) 1-
  C) 1+
  D) 3+
  E) 5+

Question 4

Determine the energy change associated with the transition from n=2 to n=5 in the hydrogen atom.
 
  A) -2.18  10-19 J
  B) +6.54  10-19 J
  C) +4.58  10-19 J
  D) -1.53  10-19 J
  E) +3.76  10-19 J

Question 5

Nitrogen dioxide reacts with water to form nitric acid and nitrogen monoxide according to the equation:
 
  3 NO2(g) + H2O(l)  HNO3(l) + NO(g)
 
  Suppose that 4 mol NO2 and 2 H2O mol combine and react completely. How many
  moles of NO are produced after the reaction has completed?
  A) 2
  B) 1.33
  C) 3
  D) 4

Question 6

Explain how an allosteric enzyme is regulated.
 
  What will be an ideal response?

[yotaSR5]

Answer to Question 1

A

Answer to Question 2

A

Answer to Question 3

D

Answer to Question 4

C

Answer to Question 5

B

Answer to Question 6

An allosteric enzyme is regulated by the interaction of some inhibitor with the enzyme at some location other than the active site. However this interaction causes some change in the active site so that the enzyme is no longer active. The biological advantage of this process is that the inhibitor does not need to be chemically similar to the substrate; instead it could be a molecule produced in a completely different process. This allows fine control of enzyme processes.

[Diane]

Gracias!

[ryansturges]

Thanks for the timely response, appreciate it