Save
Busy. Please wait.
Log in with Clever
or
show password
Forgot Password?
Don't have an account?  Sign up 
Sign up using Clever
or
Username is available taken
show password


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account. Your email address is only used to allow you to reset your password. See our Privacy Policy and Terms of Service.

Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
focusNode
Didn't know it?
click below
 
Knew it?
click below
Don't Know
Remaining cards (0)
Know
0:00
edit
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

Enzyme Kinetics

QuestionAnswer
Prosthetic group Coenzyme or metal ion that is tightly bound
Holoenzyme enzyme plus prosthetic group
Apoenzyme/apoprotein Enzyme without cofactor/coenzyme
Catalyses reactions by Degrading nutrients, conserving and transforming chemical energy and making biological macromolecules from simple building blocks
Active site A pocket within the enzyme which provides desirable environment in order to catalyse reactions
What's special about the active site? The surface of the active site is lined with amino acids with side groups that bind the substrate and participate in the chemical catalysis
What do enzymes do to the equilibrium of a reaction? They don't change the equilibrium
Enzyme kinetics How the rate of an enzyme-catalysed reaction changes in response to experimental parameters
How does the enzyme become saturated? With increasing amounts of substrate, more and more enzyme is bound by substrate and eventually the enzyme becomes saturated (all molecules are in ES form). Adding more substrate will not speed up the rate of reaction.
State the Michaelis-Menton Equation V0= Vmax[S] / Km+[S]
How is enzyme activity regulated? Via allosteric regulators that cause a change in the 3D structure of the enzyme thereby increasing or decreasing the activity of the enzyme regulating flux through a metabolic pathway
Km substrate concentration required to achieve half-maximal activity; low Km= substrate bound tightly to enzyme
Vmax rate of reaction of maximum velocity
How is Vmax and Km affected by competitive inhibition? Vmax is unaffected but Km is increased
How is Vmax and Km affected by uncompetitive inhibition Vmax is decreased but Km is decreased
How is Vmax and Km affected by non-competitive inhibition Km is unaffected but Vmax is decreased
Created by: 813890255
Popular Biochemistry sets

 

 



Voices

Use these flashcards to help memorize information. Look at the large card and try to recall what is on the other side. Then click the card to flip it. If you knew the answer, click the green Know box. Otherwise, click the red Don't know box.

When you've placed seven or more cards in the Don't know box, click "retry" to try those cards again.

If you've accidentally put the card in the wrong box, just click on the card to take it out of the box.

You can also use your keyboard to move the cards as follows:

If you are logged in to your account, this website will remember which cards you know and don't know so that they are in the same box the next time you log in.

When you need a break, try one of the other activities listed below the flashcards like Matching, Snowman, or Hungry Bug. Although it may feel like you're playing a game, your brain is still making more connections with the information to help you out.

To see how well you know the information, try the Quiz or Test activity.

Pass complete!
"Know" box contains:
Time elapsed:
Retries:
restart all cards