3rd Biochemistry Lecture Exam (Batch 2025) Flashcards
- Where and in what form in the mammalian cell is glycogen
stored?
A. mitochondrial matrix, globules
B. golgi complex, droplets
C. cytoplasm, granules
D. lysosomes, micelles
C. cytoplasm, granules
Glycogen is a branched-chain polysaccharide made exclusively from α-D-glucose. The primary glycosidic bond is an α(1→4) linkage. After an average of eight to ten glucosyl residues, there is a branch containing an α(1→6) linkage . A single molecule of glycogen can have a molecular mass of up to 108 daltons. These molecules exist in discrete CYTOPLASMIC GRANULES that also contain most of the enzymes necessary for glycogen synthesis and degradation.
(Lippincott - p. 126)
- Which is the most important function of stored liver glycogen?
A. maintain blood glucose to normal levels
B. supply dependent tissues with glucose during starvation
C. fuel reserve for synthesis of ATP when liver glycogen
stores are depleted
D. reserve buffer for energy needed for muscle activity
A. maintain blood glucose to normal levels
- Glycogen stores, although small, are extremely important.
a. LIVER GLYCOGEN - used to maintain blood glucose levels during the early stages of fasting.
b. Muscle glycogen - oxidized for muscle contraction. It does not contribute to the maintenance of blood glucose levels under any conditions.
(BRS Biochemistry - p. 2)
- Which statement is involved in synthesis of glycogen?
A. addition of glucose to the non-reducing end of a small
molecule of glycogen
B. synthesis of the protein primer
C. elongation of chains forming amylopectin chains
D. transfer of “limit dextrin” to an existing branch
C. elongation of chains forming amylopectin chains
- Which serves as a primer for glycogenesis possessing an
auto-glycosylating activity?
A. small molecule of glycogen
B. glycogenin
C. existing glycogen molecule
D. UDP-glucose
B. glycogenin
B. Primer requirement and synthesis
Glycogen synthase catalyzes the α(1→4) linkages in glycogen. This enzyme cannot initiate chain synthesis using free glucose as an acceptor of a molecule of glucose from UDPglucose.
Instead, it can only elongate already existing chains of glucose and, therefore, requires a primer. A fragment of glycogen can serve as a primer. In the absence of a fragment, the homodimeric protein glycogenin can serve as an acceptor of glucose from
UDP-glucose (see Fig. 11.5). The side-chain hydroxyl group of tyrosine-194 in the protein is the site at which the initial glucosyl unit is attached. Because the reaction is catalyzed by
GLYCOGENIN itself via AUTOGLYCOSYLATION, glycogenin is an enzyme. Glycogenin then catalyzes the transfer of at least four molecules of glucose from UDP-glucose, producing a short,
α(1→4)-linked glucosyl chain. This short chain serves as a primer that is able to be elongated by glycogen synthase, which is recruited by glycogenin, as described in C.
below. (Note: Glycogenin stays associated with and forms the core of a glycogen granule.)
(Lippincott Illustrated Reviews 8th Edition, p. 273)
- Which statement is true of the primer used for glycogenesis?
A. Has a single tyrosine residue to which glucose is added
B. A homodimer with two active sites to where glucose is
attached
C. Involves a nucleophilic attack on the outer PO4 of UDP-
glucose
D. the released PPi ensures the completion of the reaction
B. A homodimer with two active sites to where glucose is attached
B. Primer requirement and synthesis
Glycogen synthase catalyzes the α(1→4) linkages in glycogen. This enzyme cannot initiate chain synthesis using free glucose as an acceptor of a molecule of glucose from UDPglucose.
Instead, it can only elongate already existing chains of glucose and, therefore, requires a primer. A fragment of glycogen can serve as a primer. In the absence of a fragment, the HOMODIMERIC protein glycogenin can serve as an acceptor of glucose from UDP-glucose (see Fig. 11.5). The side-chain hydroxyl group of tyrosine-194 in the protein is
the site at which the initial glucosyl unit is attached. Because the reaction is catalyzed by glycogenin itself via autoglucosylation, glycogenin is an enzyme. Glycogenin then catalyzes the transfer of at least four molecules of glucose from UDP-glucose, producing a short, α(1→4)-linked glucosyl chain. This short chain serves as a primer that is able to be elongated by glycogen synthase, which is recruited by glycogenin, as described in C. below. (Note: Glycogenin stays associated with and forms the core of a glycogen granule.)
(Lippincott Illustrated Reviews 8th Edition, p. 273)
- Which reactions are needed to form UDP-glucose utilized for glycogenesis?
A. Isomerization of F6PO4 to G6PO4, hydrolysis of PPi
B. Conversion of G6PO4 to G1PO4, nucleophilic attack of
UTP’s phosphoryl O2 by G1PO4’s alpha PO4
C. Change G6PO4 to G1PO4, subsequent hydrolysis of
released PPi to 2 Pi
D. Hydrolysis of a phosphoanhydride bond & release of PPi
C. Change G6PO4 to G1PO4, subsequent hydrolysis of
released PPi to 2 Pi
A. Uridine diphosphate glucose synthesis
α-D-Glucose attached to uridine diphosphate (UDP) is the source of all the glucosyl residues that are added to the growing glycogen molecule. UDP-glucose (Fig. 11.4) is synthesized from glucose 1-phosphate and UTP by UDP–glucose pyrophosphorylase (Fig. 11.5). Pyrophosphate (PPi), the second product of the reaction, is hydrolyzed to two inorganic phosphates (Pi) by pyrophosphatase. The hydrolysis is exergonic, which ensures that the UDP–glucose pyrophosphorylase reaction proceeds in the direction of UDP-glucose production. (Note: Glucose 1-phosphate is generated from glucose 6-phosphate by
phosphoglucomutase. Glucose 1,6-bisphosphate is an obligatory intermediate in this reversible reaction [Fig. 11.6].)
(Lippincott Illustrated Reviews 8th Edition, p. 272)
- What kind of bond is formed between first glucose unit and the tyrosine residue of glycogenin?
A. glycosidic bond
B. N-linked glycosidic bond
C. O-linked glycosidic bond
D. ester-linked bond
C. O-linked glycosidic bond
N- and O-glycosides:
If the group on the non-carbohydrate molecule to which the sugar is attached is an –NH2 group, the structure is an N-glycoside and the bond is called an N-glycosidic link. If the group is an –OH, the structure is an O-glycoside, and the bond is an O-glycosidic link. [Note: All sugar–sugar glycosidic bonds are O-type linkages.]
(Lippincott Illustrated Reviews 5th Edition, p. 86)
- Which serves as substrates for UDP-glucose synthesis?
A. UTP & glucose-1-PO4
B. GTP & fructose 1-6bisPO4
C. UTP & glucose-6-PO4
D. ATP & fructose 2-6bisPO4
A. UTP & glucose-1-PO4
A. Uridine diphosphate glucose synthesis
α-D-Glucose attached to uridine diphosphate (UDP) is the source of all the glucosyl residues that are added to the growing glycogen molecule. UDP-glucose (Fig. 11.4) is synthesized from GLUCOSE 1-PHOSPHATE AND UTP by UDP–glucose pyrophosphorylase (Fig. 11.5). Pyrophosphate (PPi), the second product of the reaction, is hydrolyzed to two inorganic phosphates (Pi) by pyrophosphatase. The hydrolysis is exergonic, which ensures that the UDP–glucose pyrophosphorylase reaction proceeds in the direction of UDP-glucose production. (Note: Glucose 1-phosphate is generated from glucose 6-phosphate by
phosphoglucomutase. Glucose 1,6-bisphosphate is an obligatory intermediate in this reversible reaction [Fig. 11.6].)
(Lippincott Illustrated Reviews 8th Edition, p. 272)
- Which enzyme synthesizes UDP-glucose?
A. phosphoglucomutase
B. glycogen synthase
C. nucleoside diphosphokinase
D. UDP-Glucose-pyrophosphorylase
D. UDP-Glucose-pyrophosphorylase
A. Uridine diphosphate glucose synthesis
α-D-Glucose attached to uridine diphosphate (UDP) is the source of all the glucosyl residues that are added to the growing glycogen molecule. UDP-glucose (Fig. 11.4) is synthesized from glucose 1-phosphate and UTP by ““UDP-glucose-phosphorylase”” (Fig. 11.5). Pyrophosphate (PPi), the second product of the reaction, is hydrolyzed to two inorganic phosphates (Pi) by pyrophosphatase. The hydrolysis is exergonic, which ensures that the UDP–glucose pyrophosphorylase reaction proceeds in the direction of UDP-glucose production. (Note: Glucose 1-phosphate is generated from glucose 6-phosphate by
phosphoglucomutase. Glucose 1,6-bisphosphate is an obligatory intermediate in this reversible reaction [Fig. 11.6].)
(Lippincott Illustrated Reviews 8th Edition, p. 272)
- At least how many glucose units will be removed from a
straight chain to create a branch thru creation of an αlpha 1,6
link?
A. six
B. seven
C. eight
D. eleven
A. six
- Branch synthesis: Branches are made by the action of the branching enzyme, amylo-α(1→4)→α(1→6)-transglycosylase. This enzyme removes a set of ““six to eight”” glucosyl residues from the nonreducing end of the glycogen chain, breaking an α(1→4) bond to another residue on the chain, and attaches it to a nonterminal glucosyl residue by an
α(1→6) linkage, thus functioning as a 4:6 transferase. The resulting new, nonreducing end (see “i” in Fig. 11.5), as well as the old nonreducing end from which the six to eight residues were removed (see “o” in Fig. 11.5), can now be further elongated by glycogen synthase.
(Lippincott Illustrated Reviews 8th Edition, p. 276)
- Which is the activity of the branching enzyme of the
glycogenesis?
A. amylo α1,4 –> α1,4 glucan transferase
B. amylo α1,4 –> α1,6 transglucosidase
C. amylo α1,6 glucosidase
D. α1,4 –> α1,4 transglycosylase
B. amylo α1,4 –> α1,6 transglucosidase
IV. Glycogenolysis
B. Branch removal
Branches are removed by the two enzymic activities of a single bifunctional protein, the debranching enzyme (see Fig. 11.8). First, oligo-α(1→4)→α(1→4)-glucantransferase activity removes the outer three of the four glucosyl residues remaining at a branch. It next transfers them to the nonreducing end of another chain, lengthening it accordingly. Thus, an ““α(1→4)”” bond is broken and an α(1→4) bond is made, and the enzyme functions as a 4:4 transferase. Next, the remaining glucose residue attached in an α(1→6) linkage is removed hydrolytically by ““amylo-α(1→6)-glucosidase activity””, releasing free (nonphosphorylated) glucose. The glucosyl chain is now available again for degradation by glycogen phosphorylase until four glucosyl units in the next branch are reached.
12.Glycogen synthase action will commence after how many glucose units have been incorporated into the tyrosine residue of each of the active sites of glycogenin?
A. six
B. eight
C. nine
D. ten
B. eight
- Which is the specific reaction in the breaking down
glycogen to glucose 1-PO4?
A. nucleolysis
B. electrolysis
C. phosphorolysis
D. thiolysis
C. phosphorolysis
Glycogen phosphorylase sequentially cleaves the α(1,4) glycosidic bonds between the glucosyl residues at the nonreducing ends of the ““glycogen”” chains by simple ““phosphorolysis”” (producing ““glucose 1-phosphate””) until four glucosyl units remain on each chain at a branch point. (Lippincott Illustrated Reviews 8th Edition, p. 396)
- Which statement refers to removal of glucose as free
glucose carried out through glycogenolysis?
A. Initial removal of glucose from the reducing end of glycogen
B. Remodeling of the glycogen molecule by the use of
debranching enzymes
C. Removal of glucose units as free glucose using glycogen
phosphorylase
D. Cleavage of alpha 1,4 glycosidic links up to the branch with
alpha 1,6 bond
B. Remodeling of the glycogen molecule by the use of
debranching enzymes ???
- Glycogen phosphorylase action will stop at how many glucose units away from a branch?
A. two
B. three
C. four
D. five
C. four
IV. DEGRADATION (GLYCOGENOLYSIS)
A. Chain shortening
Glycogen phosphorylase sequentially cleaves the α(1→4) glycosidic bonds between the glucosyl residues at the nonreducing ends of the glycogen chains by simple phosphorolysis (producing glucose 1-phosphate) until ““four glucosyl units”” remain on each chain at a branch point (Fig. 11.7). The resulting structure is called a limit dextrin, and phosphorylase cannot degrade it any further (Fig. 11.8). (Note: Phosphorylase requires pyridoxal phosphate [a derivative of vitamin B6] as a coenzyme.)
(Lippincott Illustrated Reviews 8th Edition, p. 276)
- Which stimulates the inactive glycogen phosphorylase in
the muscles?
A. AMP
B. ATP
C. ADP
D. GMP
A. AMP
IV. DEGRADATION (GLYCOGENOLYSIS)
A. Allosteric regulation of glycogenesis and glycogenolysis
2. Glycogenolysis activation by AMP: Muscle glycogen phosphorylase (myophosphorylase), but not the liver isozyme, is active in the presence of the high AMP concentrations that occur under extreme conditions of anoxia and ATP depletion. AMP binds to glycogen phosphorylase b, causing its activation without phosphorylation (see Fig. 11.9). Recall that AMP also activates phosphofructokinase-1 of glycolysis, allowing glucose from glycogenolysis to be oxidized.
(Lippincott Illustrated Reviews 8th Edition, p. 284)
- In the muscles, which will convert inactive glycogen phosphorylase to the T state?
A. AMP
B. glucose 6-PO4
C. glucose
D. GTP
B. glucose 6-PO4
IV. DEGRADATION (GLYCOGENOLYSIS)
3. Glycogenolysis activation by calcium
a. Muscle phosphorylase kinase activation: During muscle contraction, there is a rapid and urgent need for ATP. It is supplied by the degradation of muscle glycogen to ““glucose 6-phosphate’”, which enters glycolysis. Nerve impulses cause membrane depolarization, which promotes Ca2+ release from the sarcoplasmic reticulum into the sarcoplasm of myocytes. The Ca2+ binds the CaM subunit, and the complex activates muscle phosphorylase kinase b (see Fig. 11.9).
(Lippincott Illustrated Reviews 8th Edition, p. 285)
- In the liver, which will convert active glycogen phosphorylase to the T state?
A. AMP
B. glucose 6-PO4
C. glucose
D. GTP
C. glucose
IV. DEGRADATION (GLYCOGENOLYSIS)
3. Glycogenolysis activation by calcium
b. Liver phosphorylase kinase activation: During physiologic stress, epinephrine is released from the adrenal medulla and signals the need for blood glucose. This ““glucose”” initially comes from hepatic glycogenolysis. Binding of epinephrine to hepatocyte α1-adrenergic GPCR activates a phospholipid-dependent cascade that results in movement of Ca2+ from the ER into the cytoplasm. A Ca2+–CaM complex forms and activates hepatic phosphorylase kinase b. Note that the released Ca2+ also helps to activate protein kinase C that can phosphorylate and inactivate
glycogen synthase a. (Lippincott Illustrated Reviews 8th Edition, p. 285-286)
- Which debranching enzyme’s activity will expose the
glucose unit linked by an α1,6 glycosidic bond?
A. amylo α1,4 –> α1,4 glucan transferase
B. amylo α1,4 –> α1,6 transglucosidase
C. amylo α1,6 glucosidase
D. α1,4 –> α1,4 transglycosylase
A. amylo α1,4 –> α1,4 glucan transferase
IV. DEGRADATION (GLYCOGENOLYSIS)
B. Branch removal
Branches are removed by the two enzymic activities of a single bifunctional protein, the debranching enzyme (see Fig. 11.8). First, oligo-α(1→4)→α(1→4)-glucantransferase
activity removes the outer three of the four glucosyl residues remaining at a branch. It next transfers them to the nonreducing end of another chain, lengthening it accordingly. Thus, an
α(1→4) bond is broken and an α(1→4) bond is made, and the enzyme functions as a 4:4 transferase. Next, the remaining glucose residue attached in an α(1→6) linkage is removed
hydrolytically by amylo-α(1→6)-glucosidase activity, releasing free (nonphosphorylated) glucose. The glucosyl chain is now available again for degradation by glycogen phosphorylase until four glucosyl units in the next branch are reached.
- Which is the sequence of enzymes used in the process of glycogenolysis?
A. alpha 1,6 glucosidase, glycogen phosphorylase, amylo 1,4 to 1,4 glucan transferase
B. glycogen phosphorylase, alpha 1,6 glucosidase, amylo 1,4 to 1,4 glucan transferase
C. amylo 1,4 to 1,4 glucan transferase, glycogen phosphorylase, alpha 1,6 glucosidase
D. glycogen phosphorylase, amylo 1,4 to 1,4 glucan transferase, alpha 1,6 glucosidase
D. glycogen phosphorylase, amylo 1,4 to 1,4 glucan
transferase, alpha 1,6 glucosidase
IV. DEGRADATION (GLYCOGENOLYSIS)
A. Chain shortening
Glycogen phosphorylase sequentially cleaves the α(1→4) glycosidic bonds between the glucosyl residues at the nonreducing ends of the glycogen chains by simple phosphorolysis (producing glucose 1-phosphate) until four glucosyl units remain on each chain at a branch
point (Fig. 11.7). The resulting structure is called a limit dextrin, and phosphorylase cannot degrade it any further (Fig. 11.8). (Note: Phosphorylase requires pyridoxal phosphate [a derivative of vitamin B6] as a coenzyme.)
B. Branch removal
Branches are removed by the two enzymic activities of a single bifunctional protein, the
debranching enzyme (see Fig. 11.8). First, oligo-α(1→4)→α(1→4)-glucantransferase
activity removes the outer three of the four glucosyl residues remaining at a branch. It next transfers them to the nonreducing end of another chain, lengthening it accordingly. Thus, an α(1→4) bond is broken and an α(1→4) bond is made, and the enzyme functions as a 4:4 transferase. Next, the remaining glucose residue attached in an α(1→6) linkage is removed hydrolytically by amylo-α(1→6)-glucosidase activity, releasing free (nonphosphorylated) glucose. The glucosyl chain is now available again for degradation by glycogen
phosphorylase until four glucosyl units in the next branch are reached.
(Lippincott Illustrated Reviews, p. 278-279)
- Which enzyme when dephosphorylated helps maintain glycogen phosphorylase inactive in the skeletal muscle?
A. protein kinase A
B. phosphorylase kinase
C. calcium calmoldulin
D. protein kinase G
B. phosphorylase kinase
???
- Which enzyme, when insulin to glucagon ratio is high, is
activated?
A. protein phosphatase
B. phosphorylase
C. phosphorylase kinase
D. protein phosphatase inhibitor
A. protein phosphatase
V. GLYCOGENESIS AND GLYCOGENOLYSIS REGULATION
A. Covalent activation of glycogenolysis
5. Phosphorylated state maintenance: The phosphate groups added to phosphorylase kinase and phosphorylase in response to cAMP are maintained because the enzyme that hydrolytically removes the phosphate, protein phosphatase-1 (PP1), is inactivated by inhibitor proteins that are also phosphorylated and activated in response to cAMP (see Fig. 11.9). Because insulin also activates the phosphodiesterase that degrades
cAMP, it opposes the effects of glucagon and epinephrine.
- Which glycogen storage disease involves a deficiency of a
unique enzyme of gluconeogenesis?
A. Pompe’s
B. von Gierke’s
C. Anderson’s
D. Her’s
B. von Gierke’s
Gluconeogenesis : Enzymes that by-pass irreversible steps
Pyruvate carboxylase
Phosphoenolpyruvate carboxykinase
Fructose-1,6-phosphatase
Glucose-6-phosphatase (Type Ia: von Gierke’s)
- Which glycogen storage disease is caused by a deficiency
of an important enzyme of glycolysis:
A. Pompe’s
B. von Gierke’s
C. Tarui’s
D. Her’s
C. Tarui’s
Glycolysis (Irreversible Steps) : Enzymes
Hexokinase/Glucokinase
Phosphofructokinase (Rate-limiting step) : Type VII : Tauri’s
Pyruvate Kinase
- Which glycogen storage disease is caused by a deficiency of muscle phosphorylase?
A. Her’s
B. McArdle’s
C. Cori’s
D. Fanconi
B. McArdle’s
- The products of the Pentose Phosphate Pathway are:
A. 2 NADPH, 1 carbon dioxide, 2 Ribose
B. 2 NADPH, 1 carbon dioxide, Ribose
C. 2 NADPH, 2 carbon dioxide, Ribose
D. 1 NADPH, 2 carbon dioxide, 2 Ribose
B. 2 NADPH, 1 carbon dioxide, Ribose
- Biosynthesis of Fatty Acids occur in the:
A. Mammary Glands
B. Ovaries
C. Adrenals
D. Liver
D. Liver
- Uses of NADPH include:
A. Degradation of Nitric Oxide
B. Oxidation of Hydrogen Peroxide
C. Phagocytosis of Red Blood Cells
D. Reductive Biosynthesis
D. Reductive biosynthesis
- A breast fed infant began to vomit frequently and lose
weight. Several days later she developed jaundice,
hepatomegaly and bilateral cataract. What is the possible
cause for these symptoms.
A. G6PD Deficiency
B. Galactosemia
C. Von Gierke’s Syndrome
D. Hereditary Fructose Intolerance
B. Galactosemia
30.The Uronic Acid Pathway:
A. Catalyzes conversion of glucose to glucuronic, pentoses,
sialic acid.
B. Energy producing reaction
C. Occurs in the cytosol
D. Alternative pathway for the oxidation of glucose
D. Alternative pathway for the oxidation of glucose
31.The rate limiting step in glycolysis is catalyzed by this
enzyme and is bypassed in the metabolism of fructose
A. Phosphofructokinase I
B. Glucose-6-Phosphate
C. Glucose-1-Phosphate
D. Glucokinase
A. Phosphofructokinase
Glycolysis (Irreversible Steps) : Enzymes
Hexokinase/Glucokinase
Phosphofructokinase (Rate-limiting step) : Type VII : Tauri’s
Pyruvate Kinase
32.Hexokinase has a low affinity for:
A. Fructose-6-Phosphate
B. Fructose-1-Phosphate
C. Fructose
D. Sucrose
C. Fructose
- Fructose-1 Phosphate reaction to Glyceraldehyde is catalyzed by:
A. Aldolase A
B. Aldolase B
C. Aldolase C
D. All of the above
B. Aldolase B
- Hereditary Fructose Intolerance is caused by a deficiency
in this enzyme:
A. Aldolase A
B. Aldolase B
C. Aldolase C
D. All of the above
B. Aldolase B
- Classic Galactosemia is caused by this enzyme deficiency:
A. GALT
B. Galactokinase
C. Galactomutase
D. Phosphogalactogen
A. GALT
- Fructose -6-Phosphate can be produced from:
A. Mannose-6-Phospate
B. Sedoheptulase-6-Phosphate
C.Xylulose-7-Phosphate
D. All of the Above
A. Mannose-6-Phosphate
- Familial fructokinase deficiency causes no symptoms
because:
A. Hexokinase can phosphorylate fructose
B. Liver aldolase can metabolize it
C. Excess fructose is excreted through feces
D. Excess fructose is converted to glucose
A. hexokinase can phosphorylate fructose
- A medical student developed hemolytic anemia after taking
the oxidizing malarial drug primaquine. This severe reaction
is most likely due to:
A. Glucose-6-phosphate dehydrogenase deficiency
B. Scurvy
C. Diabetes
D. Glycogen phosphorylase activity
A. Glucose-6-phosphate dehydrogenase deficiency
- G6PD is most severe in RBC’s because:
A.The Pentose Phosphate Pathway is the sole source of NADPH in RBC’s
B. RBC’s have nucleus and can produce ribulose-5-phosphate
C. More NADPH is needed in RBC’s to reduce glutathione
D. Glucose-6-Phosphate is consumed in RBC’s
A. The Pentose Phosphate Pathway is the sole source of NADPH in RBC’s
- True about G6PD:
A. characterized by hemolytic anemia
B. does not affect life expectancy
C. Common in Middle America, Europe, and Africa
D. symptomatic
A. Characterized by hemolytic anemia