A) C) allosteric B) D) inhibitor. competitive inhibitor. NAME, E) 48. Which tran
ID: 882195 • Letter: A
Question
A) C) allosteric B) D) inhibitor. competitive inhibitor. NAME, E) 48. Which transition-state analog. A) of the following binding constants represents the low B) Ka 1.0 10 M C) Ka x 10-10 M est affinity? D) Ka 1.0 x 109 E) Ka 5 x M Ka 2.0 x 10 M 49. 1.0 x 10 M In the established? n-catalyzed reaction given be which of the following is evidence was used to propose a mechanism for the cleavage of a peptide bond by O-C-CHit O2N p-Ni phe ylacetate p-Nitrophenol Enz OH Enz-o. C-CH3 CH, C-OH H20 Acetic acid A) Formation of a peptide bond B) Formation of an acyl-enzyme intermediate C) Elimination of water D) Hydrolytic cleavage E) B and I 50 V- k[S] represents the rate equation for the first-order reaction, where V is the velocity, S is the substrate concentration, and k is the first-order rate constant. Ifk 2000 sl, the reaction will be almost over in 10 s A) 0.5 ms B) 0.4 ms C) 0.4 s D) 0.2 sExplanation / Answer
48. Binding constant is directly proportional to the affinity so higher is the binding constant stronger is the affinity and similarly lower value of binding constant is for lower affinity, therefore in the given case,
B) 1.0 x 10^-10 M-1
will be for lowest affinity.
49. In the chymotrypsin reaction,
E) B and D
formation of an acyl-enzyme intermediate which then breaks by hydrolytic cleavage are established in the mechanism.
50. For the given first order reaction, the reaction would be almost complete in 1/2000 = 0.5 ms
So the correct answer would be,
B) 0.5 ms
Related Questions
Hire Me For All Your Tutoring Needs
Integrity-first tutoring: clear explanations, guidance, and feedback.
Drop an Email at
drjack9650@gmail.com
drjack9650@gmail.com
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.