14. The Km of a steady-state equation was experimentally derived to be equal to 6.5 mM. If the rate constant for the disappearance of the enzyme-substrate complex were both equal to 4.0 mM, which statement is TRUE about this reaction? A. The enzyme-substrate complex is permanent. B. In principle, k2 has higher magnitude than k.1. C. The reaction is kinetically possible but unstable. D. The magnitude of kı is lower compared to k2. 15. Template/lock and key theory of enzyme action is supported by which of the following? A. Enzymes speed up a reaction B. Enzymes determine the direction of a reaction C. Compounds similar to substrate inhibit enzyme activity D. Enzymes have absolute specificity to a certain substrate only E. Enzymes occur in living beings and speed up certain reactions
14. The Km of a steady-state equation was experimentally derived to be equal to 6.5 mM. If the rate constant for the disappearance of the enzyme-substrate complex were both equal to 4.0 mM, which statement is TRUE about this reaction? A. The enzyme-substrate complex is permanent. B. In principle, k2 has higher magnitude than k.1. C. The reaction is kinetically possible but unstable. D. The magnitude of kı is lower compared to k2. 15. Template/lock and key theory of enzyme action is supported by which of the following? A. Enzymes speed up a reaction B. Enzymes determine the direction of a reaction C. Compounds similar to substrate inhibit enzyme activity D. Enzymes have absolute specificity to a certain substrate only E. Enzymes occur in living beings and speed up certain reactions
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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