Question

1. which inhibition raises km?
2. which lowers both km and vmax?
3. which cannot be overcome by substrate?
4. what does aspirin acetylate?
5. what is a suicide inhibitor?
6. which binds es only?
7. which shows parallel lines on lb plot?
8. which mimics transition state?
9. which is reversible?
10. which permanently kills enzyme?

Explanation:

1. Competitive inhibitors compete with substrate for the enzyme's active site, reducing enzyme affinity for substrate, which increases \(K_M\).
2. Uncompetitive inhibitors bind only to the enzyme-substrate (ES) complex, reducing both the effective enzyme concentration for catalysis (lowering \(V_{max}\)) and the apparent substrate affinity (lowering \(K_M\)).
3. Non-competitive inhibitors bind to an allosteric site on the enzyme (or ES complex), and their effect is independent of substrate concentration, so increasing substrate cannot overcome this inhibition.
4. Aspirin is an irreversible inhibitor that acetylates the serine residue in the active site of cyclooxygenase (COX) enzymes.
5. A suicide inhibitor is a type of irreversible inhibitor that is converted to a reactive intermediate by the enzyme itself, which then covalently modifies and inactivates the enzyme.
6. Uncompetitive inhibitors exclusively bind to the enzyme-substrate (ES) complex, not the free enzyme.
7. Uncompetitive inhibition produces parallel lines on a Lineweaver-Burk (LB) plot, as it changes both \(K_M\) and \(V_{max}\) proportionally.
8. Transition state analogs are molecules that structurally resemble the high-energy transition state of an enzyme-catalyzed reaction, binding tightly to the enzyme's active site.
9. Competitive, non-competitive (pure), and uncompetitive inhibitors are all reversible, as they bind non-covalently to the enzyme/ES complex and can be displaced or removed.
10. Irreversible (including suicide) inhibitors form covalent bonds with the enzyme, permanently modifying and inactivating it.

Answer:

1. Competitive inhibition
2. Uncompetitive inhibition
3. Non-competitive inhibition
4. The serine residue in the active site of COX enzymes
5. An irreversible inhibitor that is activated by the enzyme it targets, then covalently inactivates the enzyme
6. Uncompetitive inhibitor
7. Uncompetitive inhibition
8. Transition state analog
9. Competitive, non-competitive, and uncompetitive inhibition
10. Irreversible (suicide) inhibitor