3rd Biochemistry Lecture Exam (Batch 2024) Flashcards
1.Which of the following is a common nitrogen acceptor for all reactions involving transamination?
A. α-ketoglutarate
B. Pyruvate
C. Oxaloacetate
D. Acetoacetate
A. α-ketoglutarate
The most common compounds involved as a donor/acceptor pair in transamination reactions are glutamate and α-ketoglutarate (2-oxoglutarate), which participate in reactions with many different aminotransferases.
- Which of the following molecules in NOT synthesized from Cysteine?
A. Taurine
B. Mercaptoethanolamine
C. Melanin
D. Pyruvate.
C. Melanin
Melanin is form tyrosine
- Which of the following amino acids is NOT a donor of one carbon compound?
A. Histidine
B. Tyrosine
C. Tryptophan
D. Serine
B. Tyrosine
- In mammalian cells, Ser can be a biosynthetic substrate for the synthesis of what amino acid?
A. Methionine
B. Lysine
C. Arginine
D. Glycine
D. Glycine
Precursor of Glycine is Serine
- Which is the coenzyme utilized in the synthesis of serine from glycine?
A. N5N10 methylene tetrahydrofolate
B. Tetrahydrofolate
C. Formyl tetrahydrofolate
D. Methyl tetrahydrofolate
A. N5N10 methylene tetrahydrofolate
- Dopamine is synthesized from which of the amino acids named:
A. Tyrosine
B. Tryptophan
C. Histidine
D. Methionine
A. Tyrosine (also epinephrine and norepinephrine)
- Transamination reactions require what coenzyme derived from what vitamin?
A.NAD+/Vitamin B3
B.FAD/Vitamin B2
C.Pyridoxal PO4/Vitamin B6
D.Cobalamin/Vitamin B12
C.Pyridoxal PO4/Vitamin B6
The chirality of an amino acid is determined during transamination. For the reaction to complete, aminotransferases require participation of aldehyde containing coenzyme, pyridoxal-5’-phosphate (PLP), a derivative of Pyridoxine (Vitamin B6).
- Histidine is degraded to α-ketoglutarate and is described as a:
A. Glucogenic amino acid
B. Glucogenic/ketogenic amino acid
C. Ketogenic amino acid
D. None of the choices
A. Glucogenic amino acid
- A person with phenylketonuria cannot convert:
A. Phenylalanine to isoleucine
B. Phenylalanine to tyrosine
C. Phenol into ketones
D. Phenylalanine to phenylpyruvate
B. Phenylalanine to tyrosine
Tyrosine, which is normally formed from phenylalanine by PAH, is deficient
- An example of a transamination reaction is:
A. Glutamate = hexanoic acid + NH3
B. Aspartate + hexanoic acid = glutamate + oxaloacetate
C. Aspartate + α-ketoglutarate = glutamate + oxaloacetate
D. Glutamate = α-ketoglutarate + NH3
C. Aspartate + α-ketoglutarate = glutamate + oxaloacetate
- A person with phenylketonuria is advised not to consume which of the following products?
A. Glycine containing products
B. Glucose
C. Fat containing foods
D. Aspartame
D. Aspartame
Aspartame sweetener becomes aspartic acid and phenylalanine during digestion
- Tyrosine upon degradation gives rise to acetoacetyl CoA and fumarate, therefore characterized as:
A. Glucogenic amino acid
B. Ketogenic amino acid
C. Both glucogenic/ketogenic amino acid
D. Essential amino acid”
C. Both glucogenic/ketogenic amino acid
WIFTY
- Leucine degradation generates acetoacetate, and as such is characterized as:
A.Glucogenic amino acid
B.Ketogenic amino acid
C.Both glucogenic/ketogenic amino acid
D.Essential amino acid
B.Ketogenic amino acid
LL
- Which metabolic abnormality gives rise to the serious disease phenylketonuria?
A. Homocysteine cannot be converted into methionine
B. Phenylalanine cannot be converted into tyrosine
C. Phenylalanine cannot be converted into alanine
D. Tyrosine cannot be converted into phenylalanine
B. Phenylalanine cannot be converted into tyrosine
- In Maple Syrup Urine Disease, the enzyme deficient is?
A. alpha keto acid dehydrogenase
B. Pyridoxal phosphate
C.Transaminase
D. Alkaptonuria
A. alpha keto acid dehydrogenase
The biochemical defect in MSUD involves the alpha ketoacid decarboxylase complex. Harper’s page 721
- A mutation affecting the gene that codes for the enzyme homogentisic acid oxidase results to a clinical condition known as:
A. Tyrosinemia Type I
B. Richner-Hanhart syndrome
C. Tyrosinemia Type II
D. Alkaptonuria
D. Alkaptonuria
- Tyrosinemia Type I is due to a deficiency of which enzyme?
A. Fumarylacetoacetate hydrolase
B. Phenylalanine hydrolase
C. Cystathionine β-synthase
D. Homogentisate oxidaseb.
A. Fumarylacetoacetate hydrolase
- Which of the following amino acids are used to synthesize the donor of methyl groups in methylation reactions?
A. Cy
B. Met
C. Ser
D. Ala
B. Met
Methionine is an indispensable amino acid that is required for protein synthesis, and its adenosylated product S-adenosylmethionine plays a key role in whole-body metabolism because it is the primary biological methyl donor for the synthesis of >50 metabolites and methylation reactions
- What is the fate of the SO42- (sulfate) generated in the metabolism of cysteine?
A. Incorporated into other substances
B. Liberated unchanged
C. Used in the synthesis of PAPS
D. Incorporated into glucose to form cerebrosides
C. Used in the synthesis of PAPS
- The amino acid upon action of nitric oxide synthase (NOS) gives rise to NO, an endothelial relaxing factor.
A. Asn
B. Lys
C. Asp
D. Arg
D. Arg
Arginine, together with L-Citrulin,e gives rise to Nitric Oxide, in a reaction catalyzd by nitric oxide synthase. Trans 2023, LE3.03, page 1.
- Histamine, an intermediate of histidine metabolism during an allergic reaction is synthesized by mast cells through what
reaction?
A. Decarboxylation
B. Reduction
C. Oxidation
D. Hydroxylation
A. Decarboxylation
Histamine, an intermediate of histidine metabolism during an allergic reaction is synthesized by mast cells through Decarboxylation reaction
- Removal of carboxylic group from glutamate generates a neurotransmitter known as:
A. Serotonin
B. Dopamine
C. y–amino butyric acid (GABA)
D. Neurotensin
C. y–amino butyric acid (GABA)
Trans 2023 #3.03 p.6
* γ-Aminobutyrate (GABA) functions in brain tissue
as an inhibitory neurotransmitter by altering
transmembrane potential differences.
* GABA is formed by decarboxylation of glutamate
by l-glutamate decarboxylase
- Adrenaline is synthesized from tyrosine, utilizing norepinephrine through a methylation reaction requiring;
A.S-adenosyl methionine
B.Methyl cobalamin
C.3’-phosphoadenosine-5’-phosphosulfate
D.5-deoxyadenosyl cobalamin
A.S-adenosyl methionine
S-Adenosyl methionine (SAM-e) is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM-e is produced and consumed in the liver.
- What is the source of the amino group added to aspartate to synthesize asparagine?
A. Glutamine
B. Ammonia
C. Glycine
D. Tyrosine
A. Glutamine
- Which amino acid whose carbons upon degradation give rise to fumarate?
A. Aspartate
B. Methionine
C. Glutamine
D. Arginine
A. Aspartate
The amino acid whose carbons upon degradation gthat give rise to fumarate is Aspartate.
- In glycogen, the amylose chains are formed by what kind of glycosidic
A. Alpha 1,4
B. Beta 1,4
C. Alpha 1,2
D. Beta 1,3
A. Alpha 1,4
Amylopectin is Alpha 1,4 & Alpha 1,6
- This glycosidic bond creates the branching part of amylopectin chains of glycogen
A.Alpha 1,4
B. Beta 1.4
C.Alpha 1,2
D.Beta 1,3
A.Alpha 1,4
Amylase Alpha 1,4
Amylopectin Alpha 1,4 and Alpha 1,6
- What is the key regulatory enzyme used in glycogenolysis by the cells?
A. Glycogen phosphorylase kinase
B. Amylo α-1,4 to α-1,4 glucan transferase
C. α-1,6 glucosidase
D. glycogen phosphorylase
D. glycogen phosphorylase
Glycogenolysis is the biochemical pathway in which glycogen breaks down into glucose ` phosphate and glycogen. the reaction takes place in the hepatocytes and myocytes. the process is under the regulation of 2 key enzyme: phosphorylase kinase and glycogen phosphorylase
- Glycogen phosphorylase degrades glycogen during times of fasting starting at
A. Reducing end at anomeric carbon
B. Non-reducing end at C4
C. Sixth carbon having the alcohol group
D. Branches having the alpha-1,6 glycosidic bond
B. Non-reducing end at C4
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 before a branch point
(Lippincott’s 6th ed., Chapter 11)
- Muscle glycogen phosphorylase is allosterically modified by these factors EXCEPT:
A. ATP
B. AMP
C. Glucose
D. Glucose 6-PO4
B. AMP
- What is the key regulatory enzyme used in glycogenesis by the cells?
A. Glycogen synthase kinase
B. Glycogen synthase
C. Amylo α-1,4 to α-1,4 glucan transferase
D. Amylo α-1,4 to α-1,6 glucan transferase
B. Glycogen synthase
Glycogen synthase is the principal enzyme that synthesizes glycogen. Activation of Glycogen Synthase simulates
Glycogenesis
- What is the important amino acid
residue of glycogenin that is used to initiate the synthesis of glycogen
A. Tyrosine
B. Lysine
C. Aspartate
D. Glutamine
A. Tyrosine
The protein, named glycogenin, is joined to muscle glycogen via a novel linkage involving the hydroxyl group of tyrosine, a fact of possible significance in the light of insulin’s message being transmitted by tyrosine phosphorylation.
- What is the hormone that should be in high levels in the system so that glycogenesis will be stimulated?
a. Epinephrine
b. Glucagon
c. Insulin
d. Adrenaline
c. Insulin
First, it activates the enzyme hexokinase, which phosphorylates glucose, trapping it within the cell. Insulin acts to inhibit the activity of glucose-6 phosphatase. It also activates several of the enzymes that are directly involved in glycogen synthesis, including phosphofructokinase and glycogen synthase.
- What are the two hormones that should be in high levels in the system so that glycogenolysis will be stimulated?
A. Epinephrine/glucagon
B. Adrenaline/estradiol
C. Insulin/glucagon
D. Epinephrine/insulin
A. Epinephrine/glucagon
- In the muscles, glycogen phosphorylase is transformed into the active enzyme directly by:
A. Glycogen synthase kinase
B. Protein kinase A
C. Phosphorylase kinase
D. Adenylate kinase
B. Protein kinase A
36.The active form of glycogen synthase is ______.
A. Phosphorylated
B. The tense state
C. With attached PO4 group
D. Dephosphorylated
D. Dephosphorylated
Phosphorylation catalyzed by protein Kinases.
Dephosphorylation catalyzed by protein Phosphatases.
- The active form of glycogen phosphorylase is _____.
A. Phosphorylated
B. The tense state
C. Without attached PO4 group
D. Dephosphorylated
A. Phosphorylated
Glycogen phosphorylase exists in an inactive, dephosphorylated form and in active, phosphorylated form
- In the muscles, the need for calcium and energy used for muscle contraction is coordinated by this enzyme;
A. Glycogen phosphorylase
B. Glycogen synthase kinase
C. Glycogen phosphorylase kinase
D. α-1,6 glucosidase
A. Glycogen phosphorylase
Muscle glycogen phosphorylase is present to degrade glycogen to forms of energy by means of glycolysis during muscle contractions
- When is glycogen phosphorylase kinase fully activated?
A. β subunit bound to Ca2+ & α subunit phosphorylated
B. β subunit bound to Ca2+ & α subunit phosphorylated
C. β subunit phosphorylated & Δ subunit bound to Ca2+
D. γ subunit phosphorylated & β subunit bound to Ca2+
C. β subunit phosphorylated & Δ subunit bound to Ca2+
The phosphorylase kinase is completely activated when the β and α subunits are phosphorylated by protein kinase A and the delta subunit has bound to calcium ions.
- The reaction catalysed by glycogen phosphorylase is carried out with the help of what ion?
A.Calcium
B. Hydroxyl ions
C. Hydrogen ions
D. Inorganic PO4-
A.Calcium
Calcium ion is carried out by the reaction catalysed by glycogen phosphorylation. (Harpers 30th Ed page 146)
- What is the reason why glycogen stored and utilized for energy needs of the cells is a branched glucose polymer?
A. More non-reducing ends for faster breakdown
B. More reducing ends for faster synthesis
C. Increasing the insolubility of the molecule
D. Decreasing the solubility of the polymer
B. More reducing ends for faster synthesis
Branching increases number of nonreducing ends to which new glucosyl residues are added. - Accelerates rate of glycogen synthesis.
- The product of the action of glycogen phosphorylase;
A. Glucose 6-PO4
B. Fructose 1-PO4
C. Free glucose
D. Glucose 1-PO4
D. Glucose 1-PO4
The activated glycogen Phosphorylase now catalyzes the breakdown of glycogen, releasing Glucose-1-Phosphate
- What is the main function of the degradation of glycogen in the liver?
a. To supply of energy to the liver cells
b. To maintain the level of blood glucose normal
c. To export glucose to the muscle tissue
d. To solely supply the brain with the source of energy
b. To maintain the level of blood glucose normal
Glycogenolysis, process by which glycogen, the primary carbohydrate stored in the liver and muscle cells of animals, is broken down into glucose to provide immediate energy and to maintain blood glucose levels during fasting.
- The activity of glycogen phosphorylase stops when there are how many glucosyl units from an α-1,6 glycosidic bond?
A. Two
B. Three
C. Four
D. Six
C. Four
The efficient breakdown of glycogen to provide glucose 6-phosphate for further metabolism requires four enzyme activities: one to degrade glycogen, two to remodel glycogen so that it remains a substrate for degradation, and one to convert the product of glycogen breakdown into a form suitable for further metabolism.
- When the activity of glycogen phosphorylase stops near a branching point in glycogen, what polymer of glucose is formed?
A. Amylose
B. Amylopectin
C. Maltodextrin
D. Limit dextrin
D. Limit dextrin
- What is the enzyme activated when insulin predominates in the human system that removes the phosphate groups attached to proteins after the action of glucagon?
A. Phosphodiesterase
B. Protein phosphatase
C. Adenylyl cyclase
D. Phosphatase kinase
A. Phosphodiesterase
Phosphodiesterase act on cyclic AMP (cAMP) to transform it to 5’ AMP.
- The product of glycogen breakdown in the muscle cells can’t be used by other tissues like the brain for its energy needs because of the absence of what enzyme?
A.Glucos-6-phosphatase
B.Pyruvate carboxylase
C.Glucokinase
D.PEP carboxykinase
A.Glucos-6-phosphatase
Glucose-6-phosphatase is absent from most other tissues, consequently is retained for the generation of ATP. (Berg JM, Tymoczko JL, Strer L., Section 21.1.4 ,Biochemistry. 5th ed., 2002)
- An infant was brought to the emergency room after the parents witnessed her having seizures. The child’s blood glucose was 28 mmol/L. After a thorough workup, a glycogen storage disease (GSD) was suspected, and a muscle biopsy was significant for the accumulation of dextrin, a form of glycogen with branching limited to only a few glucose molecules. Which of the following GSD is most likely the cause of hypoglycaemia and subsequent seizures?
A. Type I – von Gierke’s disease
B. Type II – Pompe’s disease
C. Type III – Cori’s disease
D. Type IV – Andersen’s disease
D. Type IV – Andersen’s disease
Andersen’s Disease is a Glycogen storage disease Type IV. It is deficient in Branching enzyme. (Trans 3.03 Page 7)
- 28 mmol/L. After a thorough workup, a glycogen storage disease (GSD) was suspected, and a muscle biopsy was significant
a. Pompe’s
b. von Gierke’s
c. Anderson’s
d. Her’s
b. von Gierke’s
Von Gierke disease - Glycogen accumulation in liver and renal tubule cells; hypoglycemia; lactic acidemia; ketosis; hyperlipemia. Enzyme deficient: Glucose-6-phosphatase. Reference: Harper’s 30th ed. Table 18-2 Page 179 - Glycogen storage Diseases