= 7. A carboxypeptidase was found to have a Km = 2.00 uM and a kcat of 150 s1 for its substrate. a. If the enzyme concen

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7 A Carboxypeptidase Was Found To Have A Km 2 00 Um And A Kcat Of 150 S1 For Its Substrate A If The Enzyme Concen 1 (57.67 KiB) Viewed 262 times

7 A Carboxypeptidase Was Found To Have A Km 2 00 Um And A Kcat Of 150 S1 For Its Substrate A If The Enzyme Concen 2 (46.65 KiB) Viewed 262 times

7 A Carboxypeptidase Was Found To Have A Km 2 00 Um And A Kcat Of 150 S1 For Its Substrate A If The Enzyme Concen 3 (42.35 KiB) Viewed 262 times

= 7. A carboxypeptidase was found to have a Km = 2.00 uM and a kcat of 150 s1 for its substrate. a. If the enzyme concentration is 0.01 uM and [S] = 5 uM, what is the maximum velocity for this enzyme and substrate pair?
b. A temperature jump study was carried out as a function of increasing substrate concentration (at constant enzyme concentration). How would you expect the relaxation time for the complex to change and why?
C. The presence of 5.00 mM of a competitive inhibitor decreased the initial rate of the reaction in part a by a factor of 2. What is the dissociation constant, Ki, for the enzyme-inhibitor complex?