• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/15

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

15 Cards in this Set

  • Front
  • Back
What is the rate equation?
V=k[S]
4 factors that influence enzymes
1) pH 2) temperature 3) enzyme concentration 4) substrate concentration
What is the Michaelis-Menton equation?
Vo=Vmax[S]/(Km+[S])
What are the three assumptions of the Michaelis-Menton equation?
1) The amount of substrate bound by the enzyme at one time is small. 2) [ES] does not change with time. (the steady-state assumption) 3) Only initial reaction rates are used in the analysis.
What is the specificity constant?
Vo=(Kcat/Km)[Et][S]
What is the Lineweaver-Burk equation?
1/Vo= Km/(Vmax[S]) + 1/Vmax
In competitive inhibition, the inhibitor binds to:
The active site of the enzyme.
In uncompetitive inhibition, the inhibitor binds to:
a site distinct from the active site and only to the ES complex.
In noncompetitive inhibition, the inhibitor binds to:
a site distinct from the active site and to the E or ES complex.
Which class of inhibitors: 1) has no effect of Vmax & 2) Increases Km
Competitive
Which class of inhibitors: 1) Decreases Vmax & 2) Has no effect on Km
Noncompetitive
When the substrate that binds also causes an allosteric conformational change this is described as:
homotropic
When the substrate that binds does not cause an allosteric conformational change, but allosteric conformational change is caused by a different modulator/effector this is described as:
heterotropic
In allosteric regulation, instead of using Km, we use a similar term called:
K0.5
The competitive inhibitor of Tetrahydrofolate (THF) is:
Methotrexate