Complete Exam Solution Manual for Biochemical Medicine
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Course
Biomedicine
Institution
Biomedicine
An enzyme _________ (can/cannot) alter the laws of thermodynamics and consequently _________ (can/cannot) alter the equilibrium of a chemical reaction. - Answers cannot; cannot
What do enzymes do? - Answers Enzymes accelerate the attainment of equilibria but do not shift their positions. The equil...
Complete Exam Solution Manual for Biochemical Medicine
An enzyme _________ (can/cannot) alter the laws of thermodynamics and consequently _________
(can/cannot) alter the equilibrium of a chemical reaction. - Answers cannot; cannot
What do enzymes do? - Answers Enzymes accelerate the attainment of equilibria but do not shift their
positions. The equilibrium position is a function only of the free-energy difference between reactants
and products.
Enzymes accelerate the reaction _______. The same equilibrium point is reached but much more quickly
in the presence of an enzyme. - Answers rate
Enzymes facilitate the formation of the __________. - Answers transition state
The interaction of the enzyme and substrate at the active site promotes the formation of the _______. -
Answers Transition state
What are three key attributes of an active site on an enzyme? - Answers 1. The active site is a three-
dimensional cleft or crevice.
2. The active site takes up a small part of the total volume of an enzyme.
3. Active sites are unique microenvironment.
Substrates are bound to enzymes by multiple __________ (weak/strong) attractions. - Answers weak
What is the Lock-and-key model of enzyme-substrate binding? - Answers In this model, the active site of
the unbound enzyme is complementary in shape to the substrate.
What is the Induced-fit model of enzyme-substrate binding? - Answers In this model, the enzyme
changes shape on substrate binding. The active site forms and a shape complimentary to the substrate
only after the substrate has been bound.
Transition state analogs - Answers A compound resembling the transition state of a catalyzed reaction;
such compounds are often potent inhibitors of enzyme-catalyzed reactions.
What is the effect of heat on enzyme activity? - Answers Enzyme activity increased with temperature
until the enzyme is denatured.
What is optimal pH? - Answers Optimal pH is the pH at which enzymes display maximal activity. Optimal
pH varies with the enzyme and is correlated with the environment of the enzyme.
Why is the optimal pH of pepsin noteworthy? - Answers Pepsin functions in highly acidic environments
of pH 1 and 2. Pepsin is a protein digesting enzyme, the optimal pH of pepsin is noteworthy because
most proteins would be denatured at this acidic pH.
,What are three reversible inhibitors? - Answers (1.) Competitive inhibitor (2.) Uncompetitive inhibitor
(3.) Noncompetitive inhibitor
The reduction in the rate of enzyme activity observed when the enzyme can bind the substrate or the
inhibitor but not both. Many _________________ resemble the substrate and compete with it for
binding to the enzyme's active site. Relief from inhibition substrate concentration is a kinetic hallmark of
___________. - Answers competitive inhibitors; competitive inhibition
Uncompetitive inhibition - Answers Inhibition distinguished by the fact that the inhibitor binds only to
the enzyme-substrate complex; their effects are not overcome by increased substrate concentration
The reduction in the rate of enzyme activity observed when an enzyme can bind its substrate and its
inhibitor simultaneously. _____________________ decrease the turnover number for an enzyme but do
not alter the KM of the enzyme; their effects are not overcome by increased substrate concentration. -
Answers Noncompetitive inhibition
Why is relief from inhibition by increasing the substrate concentration a kinetic hallmark of competitive
inhibition? - Answers Relief from inhibition by increasing the substrate concentration is a kinetic
hallmark of competitive inhibition because it is the only form of reversible inhibitors, including
competitive, noncompetitive, and uncompetitive inhibitors that can be hindered by an increase in
substrate concentration.
What is the hallmark of competitive inhibition? - Answers The hallmark of competitive inhibition is that
it can be overcome by a sufficiently high concentration of substrate.
A double-reciprocal plot of enzyme kinetics in the presence of a competitive inhibitor illustrates that the
inhibitor has no effect on ____________, but increases ______. - Answers Vmax; KM
An uncompetitive inhibitor does not affect the slope of the douple-reciprocal plot. _______ and
_________ are reduced by equivalent amounts. - Answers Vmax; KM
A double-reciprocal plot of enzyme kinetics in the presence and absence of a noncompetitive inhibitor
shows that _________ is unaltered and ________ is decreased. - Answers KM; Vmax
What does the Km value mean? - Answers Km is the concentration of substrates when the reaction
reaches half of Vmax. A small Km indicates high affinity since it means the reaction can reach half of
Vmax in a small number of substrate concentration. This small Km will approach Vmax more quickly
than high Km value.
What are the four major classes of biomolecules? - Answers carbohydrates, lipids, nucleic acids, and
proteins
Carbohydrate - Answers A saccharide, which can be an aldehyde or a ketone compound having multiple
hydroxyl groups. Also defined as an organic compound with the empirical formula (CH2O)n.
,Cooperative Effect - Answers enhanced activity resulting from cooperation between subunits of an
allosteric molecule
Heme - Answers an iron-containing molecule that occurs naturally in every single plant and animal-gives
blood its ability to carry oxygen
protoporphyrin - Answers the molecule that joins with Fe to make heme
will build up in the blood if Fe is low
Hydrolase - Answers catalyzes hydrolysis
Lyase - Answers cleaves covalent bonds
Ligase - Answers combines two molecules
Transferase - Answers transfers functional groups
Isomerase - Answers catalyzes rearrangement
Oxidoreductase - Answers electron transfer
In higher organisms, which of the following is composed with a double-stranded phosphodieste-linked
monomers?
(A.) RNA
(B.) DNA
(C.) Protein
(D.) Carbohydrate
(E.) None of the Above - Answers DNA
What gives proteins such a dominant role in biochemistry? - Answers their ability to spontaneously fold
into complex three-dimensional structures
Proteins are chiefly composed of which of the following?
(B.) the location in the cell in which the protein is located
(C.) the pH of the cytoplasm
(D.) the order of amino acids found in the sequence - Answers (D.) the order of amino acids found in the
sequence
What are the four key classes of biomolecules? - Answers Proteins, Nucleic Acids, Lipids, and
Carbohydrates
Of the biochemical macromolecules (proteins, nucleic acids, lipids and carbohydrates) which class is
chiefly responsible for catalysis of cellular processes? - Answers Proteins
Which property of lipids drives the formation of membranes?
(A.) Branching
(B.) Flavor
(C.) Hydrogen Bonding
(D.) Hydrophobicity
(E.) Linearity - Answers (D.) Hydrophobicity
What is an important function of carbohydrates in organisms? - Answers (C.) Serving as an energy source
DNA and RNA are composed of what basic biochemical compounds?
(A.) Nucleotides
(B.) Amino Acids
(C.) Lipids
(D.) Hydrocarbons
(E.) Aromatic Rings - Answers (A.) Nucleotides
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