Thanks to visit codestin.com
Credit goes to www.scribd.com

0% found this document useful (0 votes)
23 views201 pages

Biochem Lectures

The document is a comprehensive review of biochemistry, covering essential topics such as the chemical elements in biological matter, types of macromolecules, protein structure, and enzyme function. It includes sample questions related to carbohydrates, lipids, proteins, nucleic acids, and enzymes, aimed at reinforcing understanding of these concepts. Key concepts such as glycosidic bonds, protein denaturation, and the role of hydrogen bonds in DNA structure are also discussed.

Uploaded by

Diane Cruz
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
0% found this document useful (0 votes)
23 views201 pages

Biochem Lectures

The document is a comprehensive review of biochemistry, covering essential topics such as the chemical elements in biological matter, types of macromolecules, protein structure, and enzyme function. It includes sample questions related to carbohydrates, lipids, proteins, nucleic acids, and enzymes, aimed at reinforcing understanding of these concepts. Key concepts such as glycosidic bonds, protein denaturation, and the role of hydrogen bonds in DNA structure are also discussed.

Uploaded by

Diane Cruz
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
You are on page 1/ 201

Biochemistry Review

Jopeth M. Ramis, R.ChE, M.Sc., Ph.D. CLSSP


Registered Chemical Engineer
Fellow - Regenerative Medicine and Cellular Therapies
University of Nottingham
Certified Lean Six Sigma Practitioner –Institute of Management, London UK
What are the chemical elements that
form most of living biological matter?

The chemical elements that form most


of the molecules of living beings are
oxygen (O), carbon (C), hydrogen (H)
and nitrogen (N).
• Glucose and fructose are examples of

A. double sugars
B. disaccharides
C. single sugars
D. polysaccharides
Glycosidic bonds
©thoughtco.com
• (CH2O)n is the molecular formula for
which type of macromolecules?

A. Proteins
B. Lipids
C. Carbohydrates
D. Nucleic Acid
• Which of the following is NOT a
polysaccharide?

A. Glycogen
B. Starch
C. Sucrose
D. Cellulose
• What are used in animals as a source of
quick energy that can be stored in the
liver and muscles ?

A. Proteins
B. Nucleic acids
C. Carbohydrates
D. Lipids
• Sugars, starches, and cellulose belong
to which major class of biological
molecules?

A. Nucleic acids
B. carbohydrates
C. lipids
D. polypeptides
• Plants like sugar cane and sugar beets store
the energy as simple sugars. Other plants,
like corn and potatoes, store the energy as
more complex sugars called?
A. carbohydrates
B. calories
C. starches
D. cellulose
• Which macromolecule does not
dissolve in water?

A. proteins
B. lipids
C. carbohydrates
D. nucleic acids
C10 to C20 natural fatty acids capric, lauric,
myristic, palmitic, stearic and arachidic is:
"Carla, Laura & Maria Perform Silly
Antics"

©chemistrylibre
• What are the monomers of lipids?

A. Amino acids
B. Simple sugars
C. Fatty acids and glycerol
D. Nucleic acids
• Lipids are used by the body to perform all
of the following functions EXCEPT:

A. membrane structural material.


B. enzyme action.
C. insulation.
D. a rich energy source.
• What type of organic substances are
fats?

A. nucleic acid
B. carbohydrate
C. protein
D. lipids
• Fats that have fatty acids with only single
covalent bonds in their carbon skeletons
are

A. saturated
B. unsaturated
C. found in plants instead of animals
D. liquid at room temperature
• Which of the following is a polymer?

A. nucleic acid
B. fatty acid
C. Amino acid
D. Glycerol
©msuchemistry
• This biological macromolecule is
responsible for controlling the activity of the
cell, and it stores and transports genetic
information.

A. Carbohydrate
B. Nucleic acid
C. Water
D. Glucose
• What are described as the "building
blocks of Protein"?

A. Fiber
B. Lipids
C. Amino Acids
D. Nutrients
Non-polar side
chains: “Grandma
Always Visits
London In May For
Winston’s Party” (G,
A, V, L, I, M, F, W, P)

Polar side
chains: “Santa’s
Team Crafts New
Quilts Yearly” (S, T,
C, N, Q, Y)

Electrically charged
side chains:
“Dragons Eat
Knights Riding
Horses” (D, E, K, R,
H)
• Proteins are made of amino
acid .

A. monomers; polymers
B. polymers; polypeptides
C. polymers; monomers
D. monomers; molecules
• In this type of structure, most of carbonyl
groups of peptide bonds forms a hydrogen
bond with the amide nitrogen of another
peptide bond four amino acids further down
the polypeptide chain:

A. Alpha-helix
B. Beta-sheet
C. Beta-turn
D. Quaternary
• The isoelectric point of an amino acid is defined
as the pH

A. where the molecule carries no electric charge


B. where the carboxyl group is uncharged
C. where the amino group is uncharged
D. of maximum electrolytic mobility
• When the amino acid alanine (R-
group is CH3) is added to a solution
with a pH of 7.3, alanine becomes

A. a cation Isoelectric
B. nonpolar point of
alanine is
C. a zwitterions 6.00
D. an anion
• The term “SALTING IN” refers to?

A.Changes in an amino acid’s isoelectric


point.
B.Increasing the solubility of a protein in
solution by adding ions.
C.The use of a liquid bridge in an
electrochemical cell.
D. The ionization of a strong acid.
Salting Out (by solubility)
• Most proteins are less soluble at high salt concentrations, an effect
called salting out.
• The salt concentration at which a protein precipitates differs from
one protein to another. Hence, salting out can be used to fractionate
proteins.
• Dialysis can be used to remove the salt if necessary.
• The local spatial arrangement of a
polypeptide’s backbone atoms without regard
to the conformation of its side chains can be
called as

A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure
• Which of the following amino acids are
more likely to be found in a protein’s
interior away from aqueous solvent
molecules?

A. Val, Leu, Ile, Met, and Phe


B. Ser, Thr, Asn, Gln, and Tyr
C. Arg, His, Lys, Asp, and Glu
D. All of the above.
• Which of the following is (are) true of -
turns in proteins?

A. It is a 180º turn of four amino acids.


B.Glycine and proline are frequently
found there.
C.Are used as connecting turns of -
helix
D. All of the above.
• The primary stabilizing force of
protein secondary structure is:

•A Ionic bonds.
•B Covalent bonds.
•C Van der Waals forces.
•D Hydrogen bonds
• Two types of -pleated sheets can be
called:

•A parallel and antiparallel


•B left-handed and right-handed.
•C and 
•D αand β
Myoglobin Structure
• Which of the following is NOT a characteristic
of a globular protein?

•A Polypeptide chain in extended, long


sheets
• B Polypeptide chains are folded in a
spherical shape.
• C Contains several types of secondary
structure
• D Typical for regulatory proteins.
• The alpha helix found in myoglobin can
best be described as

A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Motif structure
• Some parts of a protein that have a specific
chemical structure and function are called
protein

A. chemicals
B. domains
C. subunits
D. enzymes
• One of the following is NOT usually a
force that helps to hold the monomer
units of a quaternary protein together?

A. Peptide bonds
B. Disulfide bonds
C. Salt bonds
D. Hydrophobic interactions
What is protein denaturation? Is there any
change in the primary structure when a protein
is denatured? What are some factors that can
lead to protein denaturation?

• Secondary, tertiary and quaternary structures of proteins


are spatial structures. Denaturation is modification in any
of these spatial structures that makes the protein
deficient or biologically inactive.
• After denaturation the primary protein structure is not
affected.
• Protein denaturation can be caused by temperature
variation, pH change, changes in the concentration of
surrounding solutes. Most proteins denature after certain
elevation of temperature or when in very acid or very
basic solutions.
• If a person breathes into a paper bag, you
would expect their blood CO2 to

A. decrease and their blood pH to increase


B. decrease and their blood pH to decrease
C. increase and their blood pH to increase
D. increase and their blood pH to decrease
• The quaternary structure of a protein is

A.the sequence of amino acids in the


polypeptide
B. the coiling or folding of the polypeptide
C. the intertwining of two or more polypeptides
D.the 3-dimensional appearance of the
polypeptide
• The action of disrupting the three-
dimensional shape of a protein is
termed

A. dehydration
B. denaturation
C. deamination
D. hydrolysis
Sample questions
• At a pH >pI of a given protein, that protein
becomes , at the pH<pI of that
same protein, it becomes .

negatively charged (an anion)


positively charged (a cation)

The isoelectric point (pI) is the pH at which a particular molecule or surface


carries no net electrical charge.
Sample questions
• The imino acid found in protein structure

• (a) Arginine
• (b) Proline
• (c) Histidine
• (d) Lysin
• The bonds in protein structure that are
not broken on denaturation.

• (a) Hydrogen bonds


• (b) Peptide bonds
• (c) lonic bond
• (d) Disulfide bonds
• Which of the following • What type of sugar is
is not considered a found in the
pyrimidine? nucleotides of DNA?

A. C A. deoxyribose
B. T B. ribose
C. U C. glucose
D. G D. none of the above
• What is the role of hydrogen bonds in
the structure if DNA?

A. to code for proteins


B. to synthesize proteins
C. to separate the strands
D. to connect the base pairs
Which type of chemical bond maintains the
pairing of each chain in the DNA molecule?

• To form the DNA molecule, purine bases


bind to pyrimidine bases by intermolecular
bonds called hydrogen bonds. Hydrogen
bonds occur when there is hydrogen near
one of these electronegative elements:
oxygen or nitrogen.
Sample questions for the nucleic acid section

Nucleoside is a pyrimidine or The sugar in RNA is , the


purine base sugar in DNA is

• A.covalently bonded to a • A.deoxyribose, ribose


sugar • B.ribose, deoxyribose
• B.ionically bonded to a sugar • C.ribose, phosphate
• C.hydrogen bonded to a sugar • D.ribose, uracil
• D.none of the above
Sample questions for the nucleic acid section

In gel electrophoresis, what Nucleotide bases and


fragments will move most aromatic amino acids
quickly through a gel? absorb light respectively at

• A.Large fragments • A.280 and 260 nm


• B.Small fragments • B.260 and 280 nm
• C.Large genome • C.270 and 280 nm
• D.None of these • D.260 and 270 nm
Sample questions for the nucleic acid section

Which of the following is found Which is true about the pairing of


on RNA but not DNA? bases in the DNA molecule?

• A.Uracil • A. purines always pair with


• B.Deoxyribose pyrimidines
• C.Phosphate • B. a single ring base pairs with
• D.Adenine another single ring base
• C. a double ring base pairs with
another double ring base
• D. purines pair with purines and
pyrimidines with pyrimidines
Sample questions for the nucleic acid section

A messenger acid is 336 nucleotides With what mRNA codon would the
long, including the initiator and tRNA in the diagram be able to
termination codons. The maximum form a codon-anticodon base
number of amino acids in the pairing interaction?
protein translated from this mRNA
is:
• A. 3'-AUG-5'
• A 999
• B. 3'-GUA-5'
• B 630
• C. 3'-CAU-5'
• C 330
• D. 3'-UAC-5'
• D 111
• E. 3'-UAG-5'
• E 110
Sample questions for the nucleic acid section

• Of what units are nucleic acids constituted? What are the


chemical entities that compose that unit?
• What is the rule for the pairing of nitrogenous bases in
the DNA molecule? And in the RNA?
• For each of the following structures identify: the
carbohydrate (ribose or deoxyribose)?; nucleoside or a
nucleotide? DNA or a RNA system?
Sample questions
What is the function of enzymes within living systems?
• A) structural elements
• B) neurotransmitters
• C) catalysts
• D) hormones

Enzymes have names that


• A) always end in -ase
• B) always end in -in
• C) can end either in -in or -ase
• D) can end in either -in or -ogen
Sample questions
The protein portion of a conjugated enzyme is called a(n)
• A) apoenzyme.
• B) coenzyme.
• C) holoenzyme.
• D) cofactor.

Which of the following could be a component of a conjugated enzyme?


• A) coenzyme
• B) cofactor
• C) apoenzyme
• D) more than one correct response
• E) no correct response
Sample questions
Enzyme cofactors that bind covalently at the active site of an enzyme
are referred to as .
• (a) cosubstrates.
• (b) prosthetic groups.
• (c) apoenzymes.
• (d) vitamins
Sample questions
Which of the following statements concerning the effect of temperature
change on an enzyme-catalyzed reaction is correct?
• A) An increase in temperature can stop the reaction by denaturing
the enzyme.
• B)An increase in temperature can increase the reaction rate by
increasing the speed at which molecules move.
• C)An increase in temperature to the optimum temperature
maximizes reaction rate.
• D) more than one correct response
• E) no correct response
Sample questions
• A catalyst can promote product formation during a chemical reaction
by .
• (a) lowering the activation energy barrier.
• (b) stabilizing the transition state.
• (c) positioning reactants in the correct orientation.
• (d) bringing reactants together.
• (e) all of the above

Which of the following is characteristic of an enzyme catalyst?


• (a) It positions reactants in the correct orientation.
• (b) It lowers the activation energy barrier.
• (c) It binds the transition state tighter than the substrate.
• (d) all of the above
Sample questions
An enzyme active site is the location in the enzyme where
• A) protein side groups are brought together by bending and folding
to form a site for interactions with substrates
• B) the catalyst interactions with the enzyme
• C) catalyst molecules are generated
• D) the substrate creates the catalyst molecules

An enzyme active site is the location in an enzyme where substrate


molecules
• A) are generated.
• B) become catalysts.
• C) undergo change.
• D) more than one correct response
• E) no correct response
• For the enzyme reaction A+ B = C + D, Delta Go' = + 1
kcal/mol. This reaction will proceed spontaneously in a
forward direction if:

A. The concentration of C is increased one-hundred fold


B. The concentration of A is increased one-hundred fold
C. The concentration of B is lowered one-hundred fold
D.The concentration of both A and D are increased one-
hundred fold
• Which of the following statements about enzymes or
their function is true?

A.Enzymes do not alter the overall change in free


energy for a reaction
B. Enzymes are proteins whose three-dimensional form
is key to their function
C.Enzymes speed up reactions by lowering activation
energy
D. All of the above
• What is the optimal temperature range
for the majority of enzymes?

A. 40-55 ℃
B. 35-40 ℃
C. 25-30 ℃
D. 15-20 ℃
• An allosteric activator

A. increases the binding affinity


B. decreases the binding affinity
C. stabilizes the R state of the protein
D. both (a) and (c)
• Reactants of an enzyme-catalyzed
reaction are known as

A. products
B. substrates
C. proteins
D. complex
• The location on an enzyme where
binding occurs is known as the

A. action point
B. enzyme
C. binding location
D. active site
• Enzymes catalyze reactions by

A.Increasing the free energy of the system so that the


change in free energy is positive
B.Increasing the free energy of the substrate so that it is
greater than the free energy of the product
C. Changing the equilibrium constant for the reaction
D. Decreasing the free energy of activation
• An apoenzyme

A. Includes non-protein compounds such as metal ions


B.Consists of complex organic structures which may be
classified as activation-transfer coenzymes or oxidation-
reduction coenzymes
C.Is the protein portion of the enzyme without the
cofactors
D. None of the above
• NAD+, FAD, and FMN are all cofactors
for:

A. Oxidoreductases
B. Transferases
C. Hydrolases
D. Ligases
• At the end of a chemical reaction

A. an enzyme's structure is altered


B.an enzyme is detached from the product,
has its original structure, and can catalyze
more chemical reactions
C.the enzyme loses its ablity to catallyze other
chemical reactions
D.the enzyme remains attached to the
products
Sample questions
The rate of a second order reaction depends on the concentration of
.
• (a) one substrate
• (b) two substrates
• (c) three substrates
• (d) none of the above
Rate constants and reaction order
Rate constant (k) measures how rapidly a reaction occurs

k1
A B + C
k-1

Rate (v, velocity) = (rate constant) (concentration of reactants)

v= k1 [A]
1st order reaction (rate dependent on concentration of 1 reactant)

v= k-1[B][C]
2nd order reaction (rate dependent on concentration of 2 reactants)

Zero order reaction (rate is independent of reactant concentration)


• On the following plot, N represents the curve for an
allosteric enzyme with no allosteric activators or
inhibitors added. If an allosteric activator was added,
which curve would one obtain?

A. Curve A
B. Curve B
C. Curve C
D. Curve D
• Which of the following statements about
allosteric enzymes is CORRECT?

A.The binding of substrate to any active site


affects the other active sites
B.The plot of initial velocity vs. substrate
concentration is a straight line
C. The Keq of the reaction is increased when
allosteric activator is bound
D.The enzymes contains only one polypeptide
chain
Enzyme kinetics
Sample questions
Which of the following kinetic parameters best describes how
well suited a specific compound functions as a substrate
for a particular enzyme?
• (a) Km
• (b) Vmax
• (c) kcat
• (d) kcat/Km
Short summary
• Km  substrate specificity; substrate binding

•kcat  the turnover number

• k /K 
cat m the catalytic efficiency
Sample questions
The rate-determining step of Michaelis Menten kinetics is
• A.the complex formation step
• B.the complex dissociation step to produce product
• C.the product formation step
• D.Both (a)and(c)
• Competitive inhibitor: Vmax stays the same, but Km increases
• Non-competitive inhibitor decreases the turnover number of the
enzyme rather than preventing substrate binding- Vmax decreases
but Km stays the same. This cannot be overcome with an increase
in substrate concentration.
• A competitive inhibitor of an enzyme works by

A. fitting into the enzyme's active site


B. fitting into the allosteric site of the enzyme
C.attaching itself to the substrate, thereby preventing
the enzyme from making contact with substrate
D.increasing the activation energy of the enzyme-
catalyzed reaction
• If an enzyme is described by the Michaelis-
Menten equation, a competitive inhibitor will:

A. decrease the Km and decrease the Vmax


B. decrease the Km, but not the Vmax
C. always just change the Vmax
D. increase the Km but not change the Vmax
• The most likely effect of a non-competitive
inhibitor on an Michaelis-Menten enzyme
is to

A. Increase the Vmax


B. Decrease the Vmax
C. Increase both the Vmax and the Km
D. Decrease both the Vmax and the Km
Sample questions
Which of the following binds to an enzyme at its active site?
• A) irreversible inhibitor
• B) reversible competitive inhibitor
• C) reversible noncompetitive inhibitor
• D) more than one correct response
• E) no correct response

An uncompetitive inhibitor binds to .


• (a) E
• (b) ES
• (c) P
• (d) a and b
• (e) a and c
Sample questions
A reversible inhibitor that can bind to either E alone or the ES complex
is referred to as a .
• (a) competitive inhibitor.
• (b) non-competitive inhibitor.
• (c) uncompetitive inhibitor.
• (d) suicide inhibitor.
• (e) irreversible inhibitor.
Sample questions
A competitive inhibitor of an enzyme is usually
• A.a highly reactive compound
• B.a metal ion such as Hg2+ or Pb2+
• C.structurally similar to the substrate.
• D.water insoluble

The enzyme inhibition can occur by


• A.reversible inhibitors
• B.irreversible inhibitors
• C.Both (a) and (b)
• D.None of these
Sample questions
In a Lineweaver-Burk Plot, competitive
inhibitor shows which of the following
effect?
• A.It moves the entire curve to right
• B.It moves the entire curve to left
• C.It changes the x-intercept
• D.It has no effect on the slope
Sample questions
Non-competitive inhibitor of an enzyme catalyzed
reaction
• A.decreases Vmax
• B.binds to ES
• C.both (a) and (b)
• D.can actually increase reaction velocity in rare
cases
Sample questions
A classical uncompetitive inhibitor is a compound that binds
• A.reversibly to the enzyme substrate complex yielding an
inactive ESI complex
• B.irreversibly to the enzyme substrate complex yielding an
inactive ESI complex
• C.reversibly to the enzyme substrate complex yielding an
active ESI complex
• D.irreversibly to the enzyme substrate complex yielding an
active ESI complex
Enzyme regulation
Sample questions
• Two curves showing the rate versus substrate concentration are
shown below for an enzyme‐catalyzed reaction. One curve is for the
reaction in the presence of substance X. The other curve is for data
in the absence of substance X. Examine the curves and tell which
statement below is true.
• A) The catalysis shows Michaelis‐Menten kinetics with or without X.
• B) X increases the activation energy for the catalytic reaction.
• C) X could be a competitive inhibitor.
• D) X is an activator of the enzyme.
Sample questions
Allosteric modulators seldom resemble the substrate or
product of the enzyme. What does this observation
show?
• A) Modulators likely bind at a site other than the active
site.
• B) Modulators always act as activators.
• C) Modulators bind non-covalently to the enzyme.
• D) The enzyme catalyzes more than one reaction.
Sample questions
• Some enzymatic regulation is allosteric. In such cases,
which of the following would usually be found?
• A) cooperativity
• B) feedback inhibition
• C) both activating and inhibitory activity
• D) an enzyme with more than one subunit
• E) the need for cofactors
Metabolic
Pathways
Glycolysis
Sample questions
• Glycolytic pathway regulation involves
• A. allosteric stimulation by ADP
• B. allosteric inhibition by ATP
• C. feedback, or product, inhibition by ATP
• D. all of the above

• Why does the glycolytic pathway continue in the direction of


glucose catabolism?
• A. There are essentially three irreversible reactions that act as the
driving force for the pathway
• B. High levels of ATP keep the pathway going in a forward
direction
• C. The enzymes of glycolysis only function in one direction
• D. Glycolysis occurs in either direction
Sample questions
The released energy obtained by oxidation of glucose is stored as
A. a concentration gradient across a membrane
B. ADP
C. ATP
D. NAD+
Sample questions
• For every one molecule of sugar glucose which is oxidized
molecule of pyruvic acid are produced.
• A.1
• B.2
• C.3
• D.4

• The enzymes of glycolysis in a eukaryotic cell are located in the


• A.intermembrane space
• B.plasma membrane
• C.cytosol
• D.mitochondrial matrix
Sample questions
• Which of the following is not true of glycolysis?
• A.ADP is phosphorylated to ATP via substrate level
phosphorylation
• B.The pathway does not require oxygen
• C.The pathway oxidizes two moles of NADH to NAD+ for each mole
of glucose that enters
• D.The pathway requires two moles of ATP to get started
catabolizing each mole of glucose

• ATP is from which general category of molecules?


• A.Polysaccharides
• B.Proteins
• C.Nucleotides
• D.Amino acids
Sample questions
• Which of the following regulates glycolysis steps?
• A.Phosphofructokinase
• B.Hexose kinase
• C.Pyruvate kinase
• D.All of these
Sample questions
• Which of the following is not a mechanism for altering the flux of
metabolites through the rate-determining step of a pathway?
• A. Allosteric control of the enzyme activity
• B. Block active sites
• C. Genetic control of the enzyme concentration
• D. Covalent modification of the enzyme

• Phosphofructokinase, the major flux-controlling enzyme of


glycolysis is allosterically inhibited and activated respectively by
• A.ATP and PEP
• B.AMP and Pi
• C.ATP and ADP
• D.Citrate and ATP
• Where does glycolysis occur?

A. inner membrane of mitochondria


B. matrix of mitochondria
C. stroma of chloroplast
D. cytoplasm
• Sports physiologists wanted to monitor
athletes to determine at what point their
muscles were functioning anaerobically. They
could do this by checking for a buildup of
which of the following compounds?

A. oxygen
B. ATP
C. lactate
D. carbon dioxide
gluconeogenesis
Sample questions
• There are four enzymes of gluconeogenesis that
circumvent the irreversible steps in glycolysis. When
starting with the substrate pyruvate or lactate they are
• A.Hexokinase, phosphofructokinase-1,
phosphofructokinase-2 and pyruvate kinase
• B.Pyruvate carboxylase, phosphoenolpyruvate
carboxykinase, fructose-1,6-bisphosphatase, and
glucose-6-phosphatase
• C.Glycerol kinase, glycerol-3-phosphate
dehydrogenase, fructose-2,6-bisphosphatase, and
glucose-6-phosphatase
• D.Amino transferase, phosphoenolpyruvate
carboxykinase, fructose-2,6-bisphosphatase, and
glucose-6-phosphatase
Sample questions
• The enzymes that remove phosphate groups during the
process of gluconeogenesis and circumvent two of the
three irreversible reactions of glycolysis are

• A. Pyruvate kinase and glycerol kinase


• B.Phosphoenolpyruvate carboxykinase and glycerol
kinase
• C.3-Phosphoglycerate kinase and fructose-1,6-
bisphosphatase
• D.Fructose-1,6-bisphosphatase and glucose-6-
phosphatase
Glycolysis <-> gluconeogenesis

Gluconeogenesis is not the reversal of glycolysis !!!

Glycolysis: in the cytosol

Gluconeogenesis: major part in cytosol


-> 1st step in mitochondria -> shuttle

Biotin: prosthetic
group -> carrier
for CO2

Reverse reaction of glycolysis thermodynamically


not favorable !!!
112
Sample questions
• The most important control step in gluconeogenesis is fructose-1,6-
bisphosphatase. All of the following statements are true EXCEPT

• A.Fructose-1,6-bisphosphatase converts fructose-2,6-bisphosphate


to fructose-6-phosphate
• B.During times when insulin is high, fructose-1,6-bisphosphatase is
inhibited by fructose-2,6-bisphosphate
• C.During a fast or exercise when glucagon and/or epinephrine are
high, fructose-1,6-bisphosphatase is active because of the absence
of fructose-2,6-bisphosphate
• D.Glycolysis or gluconeogenesis cannot be active at the same
time. If they were is would be a futile cycle
Sample questions
• In the liver, glucagon will activate
• A. Glycolysis and glycogen synthesis
• B. Gluconeogenesis and glycogenolysis
• C. Gluconeogenesis and glycogen synthase
• D. Gluconeogenesis and glycogen synthesis

• Which of the following statements about hormonal levels during different


states is true?
• A.During the time you are eating a high carbohydrate mixed meal, the
insulin to glucagon ratio will decrease
• B.When passing from the fed to fasting state, insulin and glucagon usually
decrease
• C. When playing basketball, epinephrine is usually low and insulin is high
• D.After running for 20 miles, epinephrine and glucagon are high and insulin
is low
Sample questions
• All of the following will result in activation of glycogen
phosphorylase in skeletal muscle EXCEPT
• A.Increased concentrations of AMP from contraction of
muscle
• B. Increased epinephrine and cAMP
• C. Increased cytosolic [Ca++]
• D. Increased protein phosphatase
• E. Increased activity of glycogen phosphorylase kinase
Oxidative phosphorylation
Sample Questions
• A biological redox reaction always involves
• A.an oxidizing agent
• B.a gain of electrons
• C.a reducing agent
• D.all of these

• Coenzyme Q is involved in electron transport as


• A.directly to O2
• B.a water-soluble electron donor
• C.covalently attached cytochrome cofactor
• D.a lipid-soluble electron carrier
Sample Questions
• FAD is reduced to FADH2 during
• A. electron transport phosphorylation
• B. lactate fermentation
• C. Krebs cycle
• D. glycolysis

• During glycolysis, electrons removed from glucose


are passed to
• A. FAD
• B. NAD+
• C. acetyl CoA
• D. pyruvic acid
Sample Questions
• Almost all of the oxygen (O2) one consumes in
breathing is converted to:
• A.acetyl-CoA.
• B.carbon dioxide (CO2).
• C.carbon monoxide and then to carbon dioxide.
• D.water.

• The carbon dioxide is primary a product of


• A.Krebs cycle
• B.glycolysis
• C.electron transport phosphorylation.
• D.lactate fermentation.
• Cellular respiration takes place
mostly in:

A. chloroplasts
B. ribosomes
C. nucleus
D. mitochondria
• Which of the following is not present
during the TCA cycle?

A. NADH
B. O2
C. CO2
D. ATP
• Which of the following is a list of the stages in
the correct order?

A.pyruvate oxidation, glyocolysis, the citric acid


cycle, and oxidative phosphorylation
B.oxidative phosphorylation, glyocolysis, the
citric acid cycle, and pyruvate oxidation
C. glycolysis, pyruvate oxidation, the citric acid
cycle, and oxidative phosphorylation
D.glycolysis, the citric acid cycle, pyruvate
oxidation, and oxidative phosphorylation
• What are the products of the citric
acid cycle?

A. NADH, ATP, FADH2, and CO2


B. O2, ADP, 1 FAD, and NAD+
C. Glucose, ATP, O2, and NADH
D. heat, H2O, NADH, and pyruvate
• Which of the following is NOT a way of
producing ATP in humans?

A. Krebs Cycle
B. Alcohol Fermentation
C. Lactic Acid Fermentation
D. Glycolysis
• Which of the following is an aerobic
product of pyruvate catabolic
metabolism?

• A lactate
• B ethanol
• C acetyl CoA
• D glucose
• The TCA cycle:

A. Is found in the cytosol


B.Is controlled by the ADP/ATP ratio and the
NADH concentration
C. Is also called the Cori cycle
D. Produces most of the water made in humans
• The Krebs Cycle begins when pyruvic acid
produced by glycolsis enters the

A. cytosol
B. air
C. mitochondrion
D. nuclear
• In aerobic organisms growing in the
presence of oxygen, the NADH produced by
glycolysis ultimately donates its high-energy
electrons to .

A.electron transport chains in the


mitochondria
B. ATP
C. pyruvate
D. glucose
• Cellular respiration takes place mostly
in:

A. chloroplasts
B. ribosomes
C. nucleus
D. mitochondria
• The main purpose of the electron transport
chain is to:

A.Use high energy electrons from other


cycles to convert ADP into ATP
B.Maintain a stable balance of high energy
electrons
C. Constantly distribute electrons throughout
the cell
D.Tell the cell when glycolysis should stop or
start
• Oxidative phosphorylation:

A. Is anaerobic
B. Requires AMP
C. Requires the electron transport system
D.Is not dependent upon development of
a proton gradient
• Where are the proteins of the electron
transport chain located?

A. cytosol
B. mitochondrial outer membrane
C. mitochondrial inner membrane
D. mitochondrial matrix
• The ATP synthase responsible for most of the
ATP synthesis in the body is located:

A.On the outer side of the outer mitochondria


membrane
B.On the inner side of the outer mitochondria
membrane
C. On the outer side of the inner mitochondria
membrane
D.On the inner side of the inner mitochondria
membrane
• In the electron transport chain, the final
electron acceptor is

A. oxygen
B. a molecule of carbon dioxide
C. a molecule of water
D. ADP
• Anemia, hemorrhage, and chronic obstructive pulmonary disease
can all cause metabolic acidosis. The best explanation is that the
lack of oxygen causes

A.a decrease in insulin that, in turn, increases anaerobic glycolysis


in the brain
B.a decrease in oxidative phosphorylation so the cells have to rely
upon anaerobic glycolysis
C.a decrease in the removal of CO2 from the blood. The resulting
decrease in pH causes an increase in glycolysis in most cells
D. an increase in glycolysis in red blood cells
• Hydrolysis of a triglyceride produces

A. many amino acids


B. different types of nucleotides
C. fatty acids and glycerol
D. monosaccharides
Amino acid metabolism
Sample question

• The site of amino acid catabolism is the:


A. Stomach
B. Small intestine
C. Large intestine
D. Liver
Sample question
• The first step in the catabolism of most amino
acids is

• A. Removal of carboxylate groups


• B. Enzymatic hydrolysis of peptide bonds
• C. Removal of the amino group
• D. Zymogen cleavage
Sample question
Which of the following is true of urea?
• A. more toxic to human cells than ammonia
• B. the primary nitrogenous waste products of
humans.
• C. insoluble in water
• D. the primary nitrogenous waste product of
most aquatic invertebrates
Sample question

A glucogenic amino acid is one which is


degraded to

• A. keto-sugars
• B. either acetyl CoA or acetoacetyl CoA
• C. pyruvate or citric acid cycle
intermediates
• D. none of the above
Sample question

Transamination is the process where

• A. carboxyl group is transferred from amino


acid
• B. α-amino group is removed from the amino
acid
• C. polymerization of amino acid takes place
• D. none of the above
Sample question
Transamination is the transfer of an amino

• A. acid to a carboxylic acid plus ammonia


• B. group from an amino acid to a keto acid
• C. acid to a keto acid plus ammonia
• D. group from an amino acid to a carboxylic
acid
Nucleic acid metabolism
Sample Question
• In inherited deficiency of hypoxanthine
guanine phosphoribosyl transferase

(A)De novo synthesis of purine nucleotides is


decreased
(B) Salvage of purines is decreased
(C) Salvage of purines is increased
(D) Synthesis of uric acid is decreased
Sample Question
• Which of the following is a required
substrate for purine biosynthesis ?

(A) 5- methyl thymidine


(B) Ribose phosphate
(C) PRPP
(D) 5-Fluoro uracil
Sample Question
• The conversion of Inosine mono phosphate

(A)To Adenosine mono phosphate (AMP) is


inhibited by Guanosine mono phosphate (GMP)
(B)To AMP requires uridine mono phosphate
(UMP)
(C) To GMP requires GMP kinase
(D) To GMP requires Glutamine
O

N
HN
Synthesis of adenine
N
and guanine nucleotides Aspartate + GTP
N
Ribose-P
IMP dehydrogenase
IMP NAD +
GDP
A.S.
synthetase NADH

COO-
IMP to AMP and GMP -OOC O

NH N
HN

N
N N
O N
Ribose-P
N N H

• Glutamine, Adenylosuccinate
Ribose-P
xanthine monophosphate
XMP
NAD, ATP used glutamine + ATP
A.S.
in GMP lyase

production fumarate Glutamate + AMP


+ PPi
O

• Aspartate, GTP
NH 2

N N
N HN
used AMP N
production N N

Ribose-P
H2N N
Ribose-P

AMP GMP
DNA replication
Sample questions
• Both strands of DNA serve as
templates concurrently in

• A. replication
• B. excision repair
• C. mismatch repair
• D. none of these
• Proofreading activity to maintain the fidelity of
DNA synthesis

• A. occurs after the synthesis has been completed


• B. is a function of the 3'-5' exonuclease activity of the
DNA polymerases
• C. requires the presence of an enzyme separate from
the DNA polymerases
• D. occurs in prokaryotes but not eukaryotes
• Which of the following repairs nicked DNA by forming a
phosphodiester bond between adjacent nucleotides?

• A. Helicase
• B. DNA gyrase
• C. Topoisomerases
• D. DNA ligase
• The replication of chromosomes by eukaryotes occurs in
a relatively short period of time because

• A. the eukaryotes have more amount of DNA for


replication
• B. the eukaryotic replication machinery is 1000 times
faster than the prokaryotes
• C. each chromosome contains multiple replicons
• D. eukaryotic DNA is always single stranded
• During which of the following process a new
copy of a DNA molecule is precisely
synthesized?

• A. Trasformation
• B. Transcription
• C. Translation
• D. Replication
• Which of the following enzyme adds
complementary bases during replication?

• A. Helicase
• B. Synthesase
• C. Replicase
• D. Polymerase
• Which of the following enzymes unwind short stretches
of DNA helix immediately ahead of a replication fork?

• A. DNA polymerases
• B. Helicases
• C. Single-stranded binding proteins
• D. Topoisomerases
• Which DNA polymerase removes RNA primers
in DNA synthesis?

• A. Polymerase I
• B. Polymerase II
• C. Polymerase III
• D. none of these
DNA polymerases are specialized for different roles in
the cell
• Enzyme, responsible for proofreading base
pairing is

• A. DNA polymerase
• B. Telomerase
• C. Primase
• D. DNA ligase
• DNA helicase is used to

• A. unwind the double helix


• B. interact the double helix closely
• C. break a phosphodiester bond in DNA strand
• D. none of the above
• The synthesis of DNA by DNA polymerase occurs in the

• A. 3' to 5' direction


• B. 5' to 5' direction
• C. 5' to 3' direction
• D. 3' to 3' direction
• The 5' and 3' numbers are related to the

• A. length of the DNA strand


• B. carbon number in sugar
• C. the number of phosphates
• D. the base pair rule
• What is the main damaging effect of UV
radiation on DNA?

• A. Depurination
• B. Formation of thymine dimers
• C. Single strand break
• D. Dehydration
Transcription
Sample questions
• Which of the following enzyme is used
for synthesis of RNA under the direction
of DNA?

• A. RNA polymerase
• B. DNA ligase
• C. DNA polymerase
• D. RNA ligase
• Which of the following is a product of
transcription?

• A. mRNA
• B. tRNA
• C. rRNA
• D. all of these
• Recognition/binding site of RNA
polymerase is called

• A. receptor
• B. promoter
• C. facilitator
• D. terminator
• An mRNA transcript of a gene
contains

• A. a start codon
• B. a stop codon
• C. a terminator
• D. all of these
• Where in the cell is the DNA transcribed into
mRNA?

• A. Cytoplasm
• B.Nucleus
• C.Golgi
• D.Cell cytoskeleton
• Since the two strands of the DNA molecule are
complementary, for any given gene:

• A. The RNA polymerase can bind to either strand.


• B.Only one strand actually carries the genetic code for a
particular gene.
• C.Each gene possesses an exact replica so that no
mutation occurs.
• D.A gene transcribed in the 5’ to 3’ direction on one
strand can be transcribed in the 3’ to 5’ direction on the
other strand.
Translation
Sample questions
• The site of protein synthesis is

• A. Ribosome
• B. Nucleus
• C. Endoplasmic reticulum
• D. Chromosome
Sample questions
• The structure in a bacterium that
indicates an active site for protein
synthesis is

• A. a chromosome.
• B. a cell membrane,
• C. a flagellum.
• D. a polysome.
Sample questions
• Which of the following is not
necessary for protein synthesis to
occur, once transcription is
completed?

• A. tRNA
• B. Ribosomes
• C. mRNA
• D. DNA
Sample questions

• During the process of translation:

• A.the peptide is ‘passed’ from the tRNA in the P-site to the tRNA in
the A-site.
• B. incoming tRNAs must first bind to the E-site.
• C.initiation begins with the binding of the ribosomal SSU to the
poly-A tail of the mRNA.
• D. the mRNA is translated by one ribosome at a time.
• The nucleolus of the nucleus is the site
where:

• A. RNA processing occurs


• B.rRNA is transcribed and ribosomal subunits are
assembled
• C. tRNA are charged with amino acids
• D. mRNA is translated into protein
Ribosome Assembly: takes place largely in a specialized domain of
the nucleus, the nucleolus
• The ribosomes are composed of

• A. proteins
• B. RNA
• C. both (a) and (b)
• D. lipids
• Which is required for protein synthesis?

• A. tRNA
• B. mRNA
• C. rRNA
• D. All of these
• In the genetic code there are:

• A. more tRNAs than codons.


• B. more codons than amino acids.
• C. more nucleotides than codons.
• D. the same number of codons and amino
acids
• the anticodon of tRNA

• A. binds to rRNA
• B. binds to an amino acid
• C. binds to the Shine Dalgarno sequence
• D. binds to an mRNA codon
• Initiation of eukaryotic translation begins when
the:

• A. large and small subunits link together, then bind to


the mRNA.
• B.ribosomal small subunit holding an initiator tRNA
binds to the 5’ end of mRNA.
• C.ribosome binds to of the start codon and an initiator
tRNA enters the ribosome.
• D.initiator tRNA binds to the start codon, followed by
binding of the ribosome large subunit.
• On the ribosome, mRNA binds

• A. between the subunits


• B. to the large subunit
• C. to the small subunit
• D. none of these
In addition to the APE sites there is an mRNA binding groove
that holds onto the message being translated
• Ribosomes select the correct tRNAs

• A. based on the aminoacyl group


• B. solely on the basis of their anticodons
• C. depending on their abundance in the
cytosol
• D. with the least abundant anticodons
• Which of the following amino acid
starts all proteins synthesis?

• A. Glycine
• B. Proline
• C. Thymine
• D. Methionine

You might also like