Enzyme 2 Flashcards
What are the four ways you can control enzyme activity?
Alter temperature
Alter chemical conditions eg pH
increase or decrease transcription or breakdown
Direct regulation of the enzyme molecule
What is cooperativity?
substrate-binding to one site increase affinity at another
An allosteric activator shifts the V [S} graph to the ….
shifts to the left
in the classic enzyme graph shape
An allosteric inhibitor shifts the V [S] graph to the ….
What is the new shape of the graph?
shifts to the right
new shape is sigmodal
What is Vmax for an allosteric inhibitor and activator compare to an average enzyme
Allosteric inhibitor has a lower Vmax
Allosteric activator has a higher Vmax
What is the effect of temp on V?
Draw a graph to explain this.
There is a slow increasing gradient.
There is an optimum temperature and after this the graph drops off fast.
What is the effect of pH on V?
Draw a graph to explain this.
pH graph looks like a mountain and it gets shifted to the left or to the right.
What is the effect of [Enzyme] on V
Explain via a graph
Positive gradient line through the origin
Remember Vmax= kcat x [E]
What are the two types of covalent enzyme regulation?
1) cleavage of peptide chain in zymogen
2) phosphorylation
Is the cleavage of peptide chain in zymogen reversible?
No
Is phosphorylation reversible?
yes
What is two non covalent method of enzyme regulation?
Reversible binding of molecules to specific sites
Increase or decease activity
State the equation to find the inhibition factor
If= 1+ [I] / Ki
Irreversible inhibitors include suicide substrates.
Name an example
aspirin
penicillin
Competitive inhibitors block what?
the binding between E + S and ES