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BIOG161 Study Guide - Modules 20-45 - Study Guide for Final

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A study guide of modules 20-45 for the course Principles of Biology I. Each module has a list of questions with the answers notated by a star. Some questions are multiple choice while others are short response. This study guide is based on course notes as well as the homework quizzes.

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Uploaded on
May 2, 2025
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KEY:
★ = correct answer
Italicized text = question
Bold and underlined text = indicates module

,#20 ATP + Activation Energy

1.)​ The high energy in the bonds that join together the phosphate groups in ATP molecules is
an example of _______

potential energy★

2.)​ What is activation energy?

the energy required to initiate a chemical reaction★

3.)​ Consider the following chemical reaction: NADH is converted to NAD+ + H+. We
would say that NADH has been…

oxidized★

4.)​ Which of the following is the lower energy, “uncharged” form?

a.) ADP ★
b.) ATP
c.) GTP
d.) NADH

5.)​ Which of the following statements best describes how ATP participates in coupled
reactions?

a.) hydrolysis of ATP fuels endergonic reactions ★
b.) synthesis of ATP fuels endergonic reactions
c.) hydrolysis of ADP fuels exergonic reactions
d.) synthesis of ADP fuels exergonic reactions

#21 Enzymes

1.)​ Which of the following statements is false? Enzymes…

a.) speed up biochemical reactions
b.) often have names that end in "ase"
c.) lower the energy of activation
d.) bind to substrates
e.) convert coenzymes to products★

, 2.)​ Which of the following statements could apply to an enzyme that has been inhibited
noncompetitively?

a.) the inhibitor molecule may be chemically and/or structurally unrelated to the substrate ★
b.) the ∆G for the reaction it catalyzes will always be negative
c.) the active site will be occupied by the inhibitor molecule
d.) more energy will be necessary to initiate the reaction
e.) raising the substrate concentration will increase inhibition

3.)​ What is the most effective way to obtain an even faster yield of product if an enzyme
solution is saturated with substrate?

add more of the enzyme★

4.)​ Which of the following characteristics is NOT associated with allosteric regulation of an
enzyme’s activity?

a.) inhibitors and activators may compete with one another
b.) a mimic of the substrate competes for the active site ★
c.) regulatory molecules bind to a site remote from the active site
d.) a naturally occurring molecule stabilizes a catalytically active conformation

5.)​ How can some bacteria survive and remain metabolically active in hot springs?

their enzymes have high optimal temperatures★

6.)​ What is the name given to the region of an enzyme where it combines with the substrate?

the active site ★

7.)​ Which of the following best describes a transition state?

a.) an interaction between reactants with high kinetic energy, due to high temperature
b.) the shape adopted by an enzyme that has an inhibitory molecule bound at its active site
c.) the complex formed as covalent bonds are being broken and re-formed during a reaction ★
d.) the place where an allosteric regulatory molecule binds to an enzyme
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