Enzyme Regulation Flashcards
What is another name for negative feedback?
Feedback inhibition
What occurs during negative feedback (or feedback inhibition)?
An end product “feedsback” and inhibits the beginning of a pathway.
(maintains homeostasis by preventing over accumulation of product)
What occurs during positive feedback?
An end product returns to the beginning of a pathway and activates it.
(increases the rate of product production)
What are the f__our types of reversible inhibitors?
- competitive
- noncompetitive
- mixed
- uncompetitive
What is the function of a noncompetitive inhibitor?
Binds to an allosteric site of an enzyme OR an E-S complex with the same affinity.
What is the function of a competitive inhibitor?
Competes with substrate for the active site of an enzyme.
The substrate and competitive inhibitor are structurally similar, that is why they both compete for the active site.
What effect does a competitive inhibitor have on Km and Vmax?
- increases Km
- NO change in Vmax
What effect does a noncompetitive inhibitor have on Km and Vmax?
- NO change Km
- decreases Vmax
[Mnemonic]
Kompetitive inhibitor: Km increases
Nonkompetitive inhibitor: NO change in Km
(how to remember the functions of a competitive and noncompetitive inhibitor)
-
Kompetitive inhibitor
- Km increases
- NO change in Vmax
-
Nonkompetitive inhibitor
- NO change in Km
- Vmax decreases
What is the function of an uncompetitive inhibitor?
When an E-S complex is formed, the active site undergoes a conformational change and creates an allosteric site. An uncompetitive inhibitor binds to that allosteric site and an E-S-I complex is formed.
What is the function of a mixed inhibitor?
Binds to either an enzyme OR an E-S complex with different affinities.
Hence why they are called “mixed”.
Which reversible inhibitor is the ONLY kind that binds to the active site of an enzyme?
Competitive inhibitor
How are the effects of competitive inhibition overcome?
By increasing substrate concentration.
If more molecules of substrate are available than molecules of inhibitor, then the enzyme will be more likely to bind to the substrate than the inhibitor.
What is kcat/Km?
A measure of enzyme efficiency.
- High kcat/ low km = high enzyme efficiency
- Low kcat/high km = low enzyme efficiency
(at saturating conditions)
What is the equation for solving Kcat?