Self-Test 103 SELF-TEST kinetics) are aproblems Enzymes and the study of enzyme
ID: 194627 • Letter: S
Question
Self-Test 103 SELF-TEST kinetics) are aproblems Enzymes and the study of enzyme reaction raesequently, mom carefully the e most dif ficult areas of biochemistry for students to ass problems have your been included in this chapter's Self-Test. If you work through theheeproblems milate Consequently understanding of this material will be greatly enhanced. Howt the answers. be beneficial if you work through them to completion without Do You Know the Terms? ACROSS s known as thenumber. At saturating substrate concentrations RyaVE 2. 4. State of a system in which no further net change is 7. The assumption that the rate of formation of ES is ex15. Molecule that binds to the The slowest reaction in a sequence is the_ -step. 11. Type of inhubitor that alters the K, of an erzyme with- out altering a occurring actly equal to the rate of breakdown of ES is called the 17. Relatively small portion of an enzyme substrate binding. (2 words) assumption (2 words)Explanation / Answer
ACROSS:
2. The slowest reaction in a sequence is RATE DETERMINE step.
4. State of a system in which no net further change is occuring: EQUILIBRIUM
7. The assumption that the rate of formation of ES is exactly equal to the rate of breakdown of ES is called the STEADY STATE assumption.
10. Kcat is known as the TURNOVER number. It measures the number of molecules of substrate which are turned over by the enzyme per second.
11. Type of an inhibitor which alters the Km of an enzyme without altering Vmax is: REVERSIBLE inhibitors.
15. Molecule that binds to the active site of an enzyme: SUBSTRATE
17. Relatively small portion of an enzyme that is involved in substrate binding: ACTIVE SITE
20. Changes in the conformation of an enzyme upon substrate binding: INDUCED FIT
21. Analog which binds more tightly to the active site than the substrate molecule: TRANSITION STATE
24. Kinetics that describe the enzymatic activity of an idealised enzyme: MICHAELIS MENTEN
25. Trypsin is to Trypsinogen as active enzyme is to : SUBSTRATE
26. Complete enzyme complex including all the protein subunits and prosthetic groups: HOLOENZYME
29. Type of energy derived from enzyme substrate interaction that lowers the activation energy of the reaction: BINDING ENERGY.
30. An enzyme without its prosthetic group: APOENZYME
31. Haemogobin without heme: APOPROTEIN
32. Common structural motifs recognised by specific protein kinases: CONSENSUS SEQUENCE.
36. Organic co-factor required for certain enzymes to be active: CO-ENZYME
37. PING-PONG MECHANISM.
38. FEEDBACK INHIBITION.
39. UREASE ENZYME.
40. CO-FACTOR.
41. ACTIVATOR.
42. REGULATORY ENZYMES.
DOWN:
1. HETEROTROPIC.
3. ENTROPY.
5. UNCOMPETETIVE INHIBITOR.
6. REACTION INTERMEDIATES.
8. GROUND STATE.
9. ACTIVATION ENERGY.
12. PROSTHETIC GROUPS.
13. TRANSITION STATE
14. DESOLVATION.
16. SUICIDE INHIBITORS.
18. TERNARY COMPLEX.
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