Enzyme Inhibition and Allosteric Regulation

Question 1

What are irreversible inhibitors?

Answer 1

inactivators
they will permenantly bind to and inactivate an enzyme, often by forming a covelnt bond. Can be powerful tooxins or drugs

Question 2

What are reversible inhibitors?

Answer 2

bind non-covalently and can dissociate, allowing the enzyme to regain activity. Can bind yo free enzyme or ES complex. Used as drugs to slow down a specific enzyme.
Are typically structural analogs of substrates or products, meaning they closely resemble the enzyme’s natural target

Question 3

Difference between uncompetitive and noncompetitive inhibition

Answer 3

Un- only binds to Es
non - binds to both free enzyme and Es complex.
Difference leads to distinct effects on Vmax and Km

Question 4

What are noncovalent modifications to an enzyme?

Answer 4

Allosteric regulation
involves the binding of small molecules to sites in the enzyme, rather than the active site

Question 5

What are covalent modification in enzyme regulation?

Answer 5

involve the formation or breakaghe of covalent bonds within the enzyme. Can be irreversible(zymogens) or reversible(phosphorylation

Question 6

What is ATCase?

Answer 6

Asparatate Transcarbamoylase. It is an
allosterically regulated enzyme in pyrimidine biosynthesis. Cooperative binding of its substrate ( binding of one substrate increases bind for another.
It is inhibited by ATP and inhibited by CTP(feedback inhibiton), Allows cell to fine-tune enzyme activity in response to the levels of specific metabolies

Question 7

WHat is the result of a positive allosteric effector?Negative

Answer 7

+ Improve enzymatic catalysis
- reduce enzyme catalysis