Which of the following accurately characterizes enzyme active sites? (Pick two.) Active sites form the greatest number of favorable electrostatic interactions with a reaction's substrates. Active sites form the greatest number of favorable electrostatic interactions with a reaction's transition state. Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site than those that resemble products or transition states. Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active site than those that resemble products or substrates.
Which of the following accurately characterizes enzyme active sites? (Pick two.) Active sites form the greatest number of favorable electrostatic interactions with a reaction's substrates. Active sites form the greatest number of favorable electrostatic interactions with a reaction's transition state. Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site than those that resemble products or transition states. Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active site than those that resemble products or substrates.
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
Problem 1P
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Transcribed Image Text:Which of the following accurately characterizes enzyme active sites? (Pick two.)
Active sites form the greatest number of favorable electrostatic interactions with a reaction's
substrates.
Active sites form the greatest number of favorable electrostatic interactions with a reaction's
transition state.
Competitive inhibitors that resemble an enzyme's substrate bind more tightly to the active site than
those that resemble products or transition states.
Competitive inhibitors that resemble an enzyme's transition state bind more tightly to the active site
than those that resemble products or substrates.
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