Biochemistry MCQs WITH SHORT EXPLANATIONS —— EE a 1. Red blood cell transketolase level is a marker for defi- ciency of: a. Vitamin BI b. Vitamin B2 & Vitamin B6 d. Vitamin BI2 Vitamin deficiencies and enzyme markers + Measurement of RBC transketolase activity isa reli able disgnostic test to assess thiamine (vitamin BI) deficiency * Assay of the enzyme RBC glutathione peroxidise will be useful in assessing riboflavin (vitamin B2) deficiency + Nanthurenic acid, produced in high quantities is excreted in urine, which serves as a reliable index (particularly after tryptophan load test) for vitamin Bé deficiency + Theexcretion of methylmalonic acid (elevated) in urine and estimation of serum B12 level are used to assess B12 deficiency. 2, Serum marker to return to normal level, last in myocar infarction is: Lactate dehydrogenase Creatine phosphokinase Aspartate transmainase |. Myoglobin Enzymes in MI ‘+ LDHis the last enzyme to rise (3-4 days) and also the last enzyme to retum to normal level in MI (10-15 days) ‘+ CPK returns to normal by 2-3 days + AST/SGOT returns to normal by 45 days ‘© Myoglobin retums to normal by 20-25 hours aoge 3. Molybdenum is a constituent of: a. Xanthine oxidase b. Cytochrome oxidase ¢. Phosphofructokinase d. Carbonic anhydrase Molybdenum containing enzymes include aldehyde ‘oxidase, sulfite oxidase and xanthine oxidase. 4. Which of the following is an important marker for myocardial infarction? a. LDH b. CK-MB ©. Troponins d._Allof the above LDH + LDHIV/H: Heart + LOHRABM + LDH: H2M2 + LDH: HMB + LDH5: Muscle (skeletal) CPK-MB + Begin to rise: 6 hours + Peak: 24 hours + Retums to normal: 48-72 hours LDH + Begin to rise: 4-6 hours # Peak: 10-24 hours + Returns to normal: 10-14 days 5. Enzymes are usually: a. Lipid b. Nucleicacids © Carbohydrates d. Protein Enzymes are mainly proteins, that catalyze chemical reactions with the exception of catalytic RNA molecules or ribozymes. 6. Other name of AST: a. SGOT b. SGPT © Alkaline phosphatase 4. Acid phosphatase SGOTIAST + Serum glutamic oxaloacetic transaminas. aminotransferase * Normally present in liver and heart cells *+ Their levels are elevated in liver damage (viral be? titis) Aspartate —dl Scanned with CamScanner: +z, \anthine Ovidase is associated with which co-factor? Copper Molybdenum Janthine oxidase «Large protein, having a molecular weight of 279000 o Rhas ¢ 2favin molevules (bound as FAD) oly’vfenum atom iron atoms bound (per enzymatic unit) § Which element is required by phosphofructokinase? 2 Magnesium Bb lnorganic phospha ce Manganese Oy Thosphotratokinate! FFK conformations In ‘dosed’ sate. the bound magnesium ion bridg the phosphooy groups of the enzyme products (ADP and fructose-L¢biphosphate) + Inopen state, the magnesium ion binds only the ADP, asthe 2 products are now further apart. 2. Troe regarding isozymes iss 2. Forms of the same enzymes that catalyze different reaction bb. Forms of the same enzymes that catalyze same reac Son Formsof the different enzymes that catalyze different reaction d. Forms of the different enzymes that catalyze same reaction ‘The multiple forms of an enzyme catalyzing the same reaction are isozymesisoenzymes, for example LDH. 40. Troponin is a marker for which of the following condi- tom: 2 Completeheartblock . Pericardial effusion © Myoglobinuria d. Myocardial infarction Troponins’Tn * Present in both skeletal and cardiac muscle, but not insmooth muscle + They differ in the way that ¢ In TnC, subunit of troponin in skeletal muscles, there are 4 calcium ion binding sites, whereas only three in cardiac muscle * TnC: Binds to calcium ions to produce a conforma- tonal change in Tal * Tal: Binds to tropomyosin, interlocking them to form 2 troponin tropomyosin complex * Th Binds to actin in thin myofilaments to hold the ‘troponin - tropomyosin complex in place. 11 Most important marker of MI: Troponin I b. CK-MB © Myoglobin 4 LOH Cantiae troponins are not enzymes, However Tropanins are now accepted ay specitic markers for myocardial infarction, Measturement of cardiac troponi fone of the main tests in early detection of episode of patient, hasbecome ischemic ischemic episode and in monitoring the Markers of Myocantial Infaretion Pins CKNS 3-8hours | 18-24 hours | 36-72 hours Troponins | 4-10hours | 18-24 hours | 8-14 days Nyogiodin— [1thows [6-7hous [24 nous 12, True for non-competitive inhibition: 2. High K, high W,. Low k.) high V,” Normal K,, low... a Normal KY high V, Enzyme inhibition + Competitive: High K,, normal V,.. + Non-competitive: Normal K,, low V,,, 13, Notan example of oxidoreductase: Hexokinase b. Cytochrome oxidase Peroxidase d, Alcohol dehydrogenas Hexokianse belongs to ‘transferases’ group 14. Which ofthe following enzyme use copper as coenzyme? a. Superoxide dismutase b. Lysyl oxidase Carbonic anhyd d._ Alkaline phosphatase Lysyl oxidase (LOX) Also known as proteit the LOX gene * Its inhibition can cause lathyrism, but, at the same time, its upregulation by tumour cells may promote ‘metastasis of the existing tumor, causing it to become malignant and cancerous. ‘+ LOX genes located on chromosome 54, # The carboyyterminus contains the active copper (II) ion, lysine, tyrosine, and cysteine residues that com- prise the catalytically active site. (PN 15, V,,, unchanged, increased K,,is seen in: a.”"Competitive inhibition Noncompetitive inhibition Allosteric regulation d. Suicide inhibition In case of competitive inhibition, the K,, is increased in presence of competitive inhibitor. In other words, the affinity of the enzyme towards substrate is apparently decreased in presence of the inhibitor. But V,,, is not changed. we -oxidase, encoded by Scanned with CamScannerStor 16. Isoform of LDH in skeletal muscle: a. LHS b. LDH2 c LDHS LDH LOWS + Constitute 5% in human serum ‘+ Originates from skeletal muscle + Destroyed at 60° C for 30 minutes + Slowest electrophoretic mobility at pH 86 ‘Subunit make up of isoenzyme is M4 17. Which of the following is a true statement regarding enzymes? 2 Inruncompettive inhibition, K, unchanged! BY Vy increased b. In uncompetitive inhibition, K,, unchanged by V,., changed c._ In uncompetitive inhibition, K,, and V,,,, increase variable . . In competitive inhibition, V,,, unchanged but K,, increased Competitive inhibition * The K, is increased in the presence of competitive inhibitor. Thus competitive inhibitor apparently increases the K,, In other words, the affinity of the enzyme towards substrate is apparently decreased in the presence ofthe inhibitor + But V,., isnot changed. 18. Which of the following enzyme does NOT require cop- perfor action? 2. Carbonic anhydrase b. Tyrosinase © Superoxide dismutase d, Ceruloplasmin More than 300 enzymes are zinc dependent. Some important ones are carboxypeptidase, carbonic anhydrase, alkaline phosphatase, lactate dehydrogenase, ethanol dehydrogenase and glutamate dehydrogenase. 19, True regarding irreversible non-competitive inhibition: a. Lower V., b. LowerK,, V,,, unchanged Affect both K, and V,,., In non-competitive inhibition, the inhibitor combines with the enzymes by forming a covalent bond and then the reaction becomes irreversible. The velocity (V,.,) is reduced. But the K, value is not changed, because the remaining enzyme molecules have the same affinity for the substrate. Cee eae eee eee 20. Metabolism of which of the following amino acid is at fault in Hartnup's disease: a. Tryptophan b. Sulfur amino acids < Glycine d. Histidine Abnormal metabolism of amino acids and conditions * Hartnup’s disease is a hereditary disorder of trypto- phan metabolism * Sulfur amino acids (methionine, cysteine and cystine) metabolism disorder results in cystinuria, cystinosis, homocystinuria and cystathionuria «© Disorder of glycine metabolism results in glycinuris 21, Hartnup’s disease is associated with increased urinary 2, 24, excretion of a. Tryptophan fc. Glycine b. Omithine d. Cystine Hartnup's disease is characterized by low plasma levels of tryptophan and other neutral amino acids and their elevated urinary excretion. Vasodilator Nitric oxide is derived from which of the following: a. Proline ‘ Derivatives of amino acids * Proline is converted to glutamate (by a series of steps) and then transaminated to alpha-ketoglutarate «+ Histidine on decarboxylation, gives the corresponding amine i. histamine + Arginine is the substrate for the production of nitric ‘oxide (NO), Precursor of tyrosine is: a. Cysteine ©. Tryptophan Amino acids and products * Cysteine forms glutathione, taurine etc. ‘+ Histidine forms histamine + Tryptophan forms serotonin, melatonin ete. * Under normal circumstances, the degradation of phenylalanine mostly occurs through tyrosine. Phe- nylalanine is hydroxylated at para-position by pher lalanine hydroxylase to produce tyrosine (p-hydroxy phenylalanine). Enzyme defective in Maple syrup urine disease is: a. Tyrosinase b. Phenylalanine hydroxylase © Branched chain alpha ketoacid dehydrogenase 4d. Homogentisate oxidase b. Histidine d._ Lysine b. Histidine d. Phenylalanine Enzyme deficiencies and conditions + ‘Tyrosinase is deficient in albinism * Phenylalanine hydroxylase is deficient in phenytke- jonuria * Maple syrup urine disease is due to.a defect in the en- zyme branched chain alpha-keto acid dehydrogenase * Homogentisate oxidase is deficient in alkaptonuria Blackening of urine on exposure to atmosphere is ob- served in: Phenylketonuria Maple syrup urine disease Hartnup disease dd. Alkaptonuria nee Scanned with CamScanner| i | | ' | | 1 : tptonariayBac urine disease Aleaplonaria isa rare inherited genetic disorder of phenylalanine ta isine metabligm, heya 4 Thisisan autosomal recessive condition that is due to adefectin the enzymehomogentisate 1,2-dioxygenase, ‘which participates in the degradation of tyrosine. «Asa result, homogentisic acid and its oxide, called alkapton, accumulate in the blood and are excreted jnurine in large amounts (hence -uria) «Excessive homogentisic acid causes damage to carti- lage (ochronosis, leading to osteoarthritis) and heart valves as well as precipitating as kidney stones + Treatment with nitisinone, which suppresses homogentisic acid production, is being studied “The apecimen bn the let, which has been ‘After two standing for hours, the fiteen minutes, tring is ‘shows some entirely darkening atthe: ‘surface, due 10 the oxidation jen midion showing blackish discoloration Le sid, urine of akaptonuria Right side alkatone bodies deposited in vertebral disc of patent 26, Glutamate is NOT a precursor of: a. GABA b. Proline © Glutathione d. Histidine Glutamate «+ Itisone of the most metabolically active of all amino acids. + Itisa precursor to: + Glutamine, Arginine, + Creatine phosphate, + Proline, . . . Hydroxyproline, Polyamines, Glutathione, and + Gamma-aminobutyric acid (GABA). * GABA, is a neurotransmitter, and is also involved in the synthesis of glutathione. + Inaddition, glutamate itself is a neurotransmitter 27, Melanin is synthesized from: ‘Tryptophan b. Tyrosine © Methionine . Taurine ‘Tyrosine as precursor * The pigment melanin. . Indopaminergiccellsin the brain tyrosines converted tolevodopaby the enzyme tyrosine hydroxylase (TH)- # THis the rate-limiting enzyme involved in the synthesis ofthe neurotransmitter dopamine. ‘* Dopamine can then be converted into the catecholamines norepinephrine (noradrenaline) and epinephrine (adrenaline), ‘The thyroid hormones triiodothyronine (T3) and thyroxine (T4) in the colloid of the thyroid also are derived from tyrosine. 28. Essential amino acid is: a. Phenylalanine b. Proline © Glutamine d. Serine Phenylalanine + Itisan alpha-amino acid. ‘+ This essential amino acid is classified as nonpolar because ofthe hydrophobic ature ofthe benz side + L-Phenylalanine (LPA) isan electrically neutral amino acid ‘+ The codons for L-phenylalanine are UUU and UUC. ‘+ Phenylalanine is a precursor for tyrosine, the mono- ‘amine signaling molecules dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline) and the skin pigment melanin. Glutamine Glutamine = Ibis the most abundant naturally occurring, non- essential amino acid in the human body and one of the only aminoacids which directly crosses the blood- brain barrier. Inthe body itis found circulating in the blood as well as stored in the skeletal muscles. ‘= One key function of glutamine isto sequesterammonia ina non-toxic form + Glutamate also plays an important role in the body's disposal of excess or waste nitrogen : ‘+ Glutamate undergoes deamination, an oxidative reac- tion catalysed by glutamate dehydrogenase. «Ammonia (as ammonium) is then excreted predomi- synthesised in the liver. nantly as urea, }. Thyroxine is synthesized from: a. Phenylalanine b, Tryptophan Tyrosine dd. None of the above Tyrosine «= Indopaminergic cellsin the brain, tyrosine is convert- ced to levodopa by the enzyme tyrosine hydroxylase (TH), TH is the rate-limiting enzyme involved in the synthesis of the neurotransmitter dopamine. «Inthe adrenal medulla, tyrosine is converted into the catecholamine hormones norepinephrine (noradrena- line), and epinephrine. + The thyroid hormones triiodothyronine (13) and thyroxine (T8) in the colloid of the thyroid also are derived from tyrosine. Scanned with CamScannerTemerks int in the urine 31. In intermittent porphyria, what is prese a. Biliverdin b. Uroporphyrin © Porphobilinogens d._Bilirubin Porphyria | * Urine estimation of porphobilinogen (PBG) is the first step if acute porphyria is suspected. ‘+ In nearly all cases of acute porphyria urinary PBG is markedly elevated except for the very rare ALA dehydratase deficiency or in patients with symptoms due to hereditary tyrosinemia type I. yndromes, 32, Essential amino acids are named so: a. Because they are produced in the body b. Because they are not produced in the body They are not important for life d._ Every food stuff essentially contains them Essential amino acids + Theyaresocalled not because they are more important to life than the others, but because the body does not synthesize them, making it essential to include them in one's diet in order to obtain them. + Leucine, Arginine, Histidine, Isoleucine, Meyhionine, Phenylalanine, Threonine, Tryptophan, Valine and lysine. * Additionally, cysteine (or sulphur-containing amino acids), tyrosine (or aromatic amino acids), histidine and arginine are required by infants and growing, children, 33. Niacin is synthesized from: a. Phenylalanine b. Tryptophan Tyrosine . Methionine Niacin * The liver can synthesize niacin from the essential amino acid tryptophan, but the synthesis is extremely inefficient; 60 mg of tryptophan are required to make ‘one milligram of niacin. + The5-membered aromatic heterocycle ofthe essential amino acid, tryptophan, is cleaved and rearranged with the alpha amino group of tryptophan into the ‘6-membered aromatic heterocycle of niacin 34. True regarding glutamine is: a. NHB transporter . Cannot cross the blood brain barrier Toxic substance in the body d. Stored in smooth muscle Glutamine functions + Assubstrate for DNA synthesis 5 Major olen protein synthesis * Glutamine has also been taken to enhance brai function as it fuels tw: peret eerie rears fuels two ofthe brains most important * Glutamic acid and * Gamma-aminobutyric acid (GABA), ems ‘One key function of the glutamine is to sequester ; form. serene inntrogea transportation and reduces to build up of ammonia in the brain (though is cont, jndicated for those with Reye's Syndrome). 5. of nitrogen in urea cycle is: 3 Se amote and aspartate b. Glutamate and NH3 Arginine and aspartate d. NHB and aspartate thine cycle or ores ereleforithine cycle is acycleot biochem reactions that produces urea from ammonia, + Inmammals, the urea cycle takes place only in the iver + The urea cycle consists of five reactions, The cycle converts two amino groups, one from NH and one from Aspartate, and a carbon atom from HCO, to relatively nontoxic excretion product, urea, at the cost of four “high-energy” phosphate bonds. The ‘equation can be summarized as 2.NH3+CO2 +3 ATP +H20 —> urea + 2 ADP +4) +AMP+2H Nitrogen donors in the urea cycle are ammonia and aspartate. 36. C peptide is part of: a. Pro-insulin b. Insulin © ACTH 4. Growth hormone C-peptide * It is a peptide that is made when proinsulin is split into insulin and C-peptide. ‘+ Cpeptide is the abbreviation for “connecting peptide”, although its name was probably also inspired by the fact that insulin is also composed of an “A” chain and 2°B" chain * It should not be confused with C-reactive protein or Protein C. 37. Glutathione is: a. Dipeptide b. Oligopeptide «. Tripeptide d. Polypeptide Glutathione (GSH) + Iisa tripeptide * Itcontains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain, * Glutathione, an antioxidant, helps protect cells from Teactive oxygen species such as free radicals andpet” oxides. * Glutathione is not an essential nutrient since it can be synthesized from the amino acids L-cysteine, L- glutamic acid and glycine, 38. True regarding ubiquitin i 2. Product of purine metabolism b. Protein destructions © Present in prokaryotes 4. Protein synthesis Scanned with CamScanner— wo Fahways of protein degradation THe pe involves lysosomal proteases and does not re- quiee ATP. “ dhe other way involves ubiquitin and is ATP-de- pendent. est indicator of protein quality is: Beet protein utilization E. Digestibility coefficient © Biological value Amino acid score ‘et protein utilization/NPU + Ratio of amino acid converted to proteins to the ratio of amino acids supplied «+ Ranges from 1 t0 0 4+ Value ofl indicates 100% utilization of dietary nitrogen as protein. Limiting amino acid in wheat are: a. Lysine, arginine b. Threonine, methionine Lysine, threonine 4. Lysine, methionine Foodstuffs and limiting amino acids + Wheat-Lysine most deficienct) and threonine (second limiting AA) + Rice: Lysine + Legumes: Tryptophan/ methionine/ cysteine + Maize: Lysine and tryptophan + Egg: None Secretory proteins are synthesized in: a. Cytoplasm ’, Endoplasmic reticulum © Both ofthe above 4. None ofthe above Secretory proteins * Secreted by a cell * May be exocrine or endocrine * Synthesized in endoplasmic reticulum ‘2. Pulses are deficient in: & Lysine b. Methionine © Both d._ None of the above Pulses/legumes are deficient in methionine. ‘©. Tyrosine becomes essential in which of the following condition: & Wilsons disease © Thyrosinosis, Phenylketonuria/PKU * Patients should keep their intake of phenylalanine (PA) ‘xtremely low to prevent mental retardation and other + pilbsic complications ut PA is the precursor for tyrosine synthesis and «Rata peels orate asics {yrosine should be supplied in diet and becomes ‘sential in the diet of PKU patients. > a. b. Alkaptonuria i. Phenylketonuria 44, Mousy odour urine is present 45, 46. 47, 48, 49, 50. Eno m a. Phenylketonuria b. Maple syrup urine disease c. Tyrosinemia 4. Homocystinuria Mousy/musty odour of urine is present in PKU as Phenylacetic acid/PAA conjugates with glutamine and excreted as phenyl acetyl glutamine. Which of the following is found in urine in Hartnup’s disease pateints? a. Phenyalanine b. Ornithine c Cystine d. Glycine Hartnup’s disease is characterized by low plasma levels of tryptophan and other neutral amino acids and their elevated urinary excretion. ‘The most direct precursor of taurine is: a. Glycis b. Cysteine © Methionine dd. Glutathione Taurine, glutathione, coenzyme A are specialized products contributed by cysteine. Which of the following is the precursor of adrenaline and noradrenaline? a. Phenylalanine ©. Tryptophan Tyrosine is the contributing amino acid for the formation of thyroxine, triiodothyronine, epinephrine, norepinephrine, dopamine and melanin. b. Tyrosine d. None of the above Norepinephrine to epinephrine conversion requires which enzyme? a. Phenylethanolamine-N-methyltransferase b. Transaldolase ¢. Tyrosine hydroxylase d. Alpha ketoglutarate Phenylethanolamine N-methyltransferase (PNMT) * Itisan enzyme found in the adrenal medulla that con- verts Norepinephrine (Noradrenaline) to Epinephrine (Adrenaline) * PNMT is positively influenced by cortisol, which is produced in the adrenal cortex. * S-adenosyl-L-methionine (SAM) is a required cofac- tor Ochronosis is seen a. Alkaptonuria b. Cystinosis cc Maplesyrup diseased. Homocystinuria Alkapton deposition occurs in connective tissues, bones and various organs (nose, ear etc.) resulting in ochronosis Which of the following substance gets deposited in connective tissue in alkaptonuria? a. Phenylacetate b. Xanthurenate c. 5-Hydroxy indole acetate d, Benzoquinone acetate Scanned with CamScanner 147 ~Alkaptonuria + Itisdueto the deficiency of homogentisic acid oxidase + Resulting in accumulation in the tissues of homogen- tisic acid, an intermediate metabolite of phenylalanine and tyrosine metabolism. + Ashomogentisicacid accumulates both intracellularly and extracellularly, it is oxidized to benzoquinone acetate, which polymerizes to form melanin-like poly ‘mers, resulting in widespread deposition in fibrous tissue and cartilage. 51, Which of the following reaction occur both in mitochon- dria and cytosol? a. Urea Cycle b. Glycolysis c. Cholesterol Synthesis d, TCA Cycle Urea synthesis is a 5 step cyclic process, with 5 distinct enzymes. “The first 2enzymes are present in mitochondria while the rest are localized in cytosol ec ee 52, Amino acid involved in urea synthesis: a. Glutamine b. Aspartic acid Valine d. Phenylalanine Urea has 2 amino (-NH2) groups, one deriv and other from aspartate. 53. A child presented to the clinic with complaints of mental retardation. Phenyllactate, phenylketone ang phenylacetate was detected in urine. Which test shoul be done? a. Gethardt’s test b. Marsh test c. Guthrie test dd. Rothera’s test Guthrie est isa rapid screening test for phenylketonuria which presents classically as mental retardation (an 1Q of 50) and excretion of phenylketone (phenylpyruvate) phenyllactate and phenylacetate in urine, from NI Pers roe Clini ice ety rd Phenyl ketonuria | Phenylalanine MR, | Phenyl hypertonia, | Phenylalanine Dietary Restriction (ype) hydroxylase seizure pyruvate, of Pho ‘Alkeptonuria Homogentisic ‘Artis, Homogentisic acid | Homogentisic acid | Nil acid oxidase cartlage Maple syrup urine | Branched chain keto | MR; Maple syrup | Val; Leu; lle; keto | Val, Leu; le; keto | Restrict Val; Leu le disease ‘acid decarboxyiase | odor, acidosis acids acids ‘Methyimalonic ac- | Methyl malonyl CoA | MR: ketosis; hypo- | Methyl malonic acid | Methyl malonic acid; | Vitamin mutase tonia ketonebodies 8, ystathionase Benign Cystathionine Cystathionine None required Carbamoyl phos- | Vomiting; ‘Ammonia; Glutamine do phate synthetase! | lethargy glutamine Transporter Pellagra ‘Aromatic amino High protein, niacin acids 54. Most specific test for HIV detects: a. RNA b. DNA. Proteins d. Nucleic acids Most specific test for HIV is Western Blot test. In this technique, proteins (not nucleic acid) are identified. 55. Collagen type Il is predominantly found in: a. Lung b. Skin © Cartilage d. Vascular tissues 56. Proteins which are synthesized in rough endoplasmic reticulum will NOT go to: a. Mitochondria c Lysosome 57. Enzyme deficient in phenylketonuria: Tyrosine hydroxylase Homogentisate oxidate Phenylalanine hydroxylase Tyrosine transaminase poop b. Golgi body d. Cytosol Mitochondria are the powerhouse of the cell, wher? energy released from oxidation of the foodstufls is trapped as chemical energy in the form of ATP. Scanned with CamScannerPKU is the MC metabolic disorder in amino acid ‘metabolism with an incidence of 1 in 10,000 births. It is due to deficiency of the hepatic enzyme, phenylalanine hydroxylase, caused by an autosomal recessive gene 58, Which enzyme is needed for phenylalanine to tyrosine conversion? ‘a. Homogentisate oxidase b. Tyrosine hydroxylase Phenylalanine hydroxylase d. Tyrosine transaminase Phenylalanine is hydroxylated at para-position by phenylalanine hydroxylase to produce tyrosine (p hydroxy phenylalanine). 59, Transamination requires: a. FAD b. Biotin © NADH 4. Pyridoxal phosphate All transaminases (aminotransferases) require pyridoxal phosphate (PLP), a coenzyme derived from vitamin BG. ©. Main bond in primary structure of protein: a. Hydrophobic interaction b. Hydrogen bond © Ionic bonds 4. Covalent peptide bonds Proteins structure ‘+ Amino acids (in primary structure) are held together by covalent peptide bonds/linkages + Secondary + Alpha helix is stabilized by extensive hydrogen bonding, + Beta pleated sheet is composed of two or more segments of fully extended polypeptide chains (hydrogen bonds) * Tertiary and quaternary structures of protein are stabi- lized by non-covalent bonds such as hydrogen bonds, hydrophobic interactions, ionic bonds. Which of the following is a non-protein amino acid? a Lysine >. Phenylalanine © Leucine 4. Taurine ‘The 20 standard amino acids can be incorporated into Proteins due to the presence of universal genetic code. Some ofthese amino acids undergo specific modification after the protein synthesis occurs. ° Whatis needed to synthesize norepinephrine and epi- ephrine? & Cysteine Tryptophan Tyrosine Phenylalanine 4. 66. Eee Norepinephrine is formed by hydroxylation and decarboxylation of tyrosine, and epinephrine by methylation of norepinephrine. Phenylethanolamine-N- methyltransferase (PNMT), the enzyme that catalyzes the formationof epinephrine from norepinephrine, is found in appreciable quantities only in the brain and the adrenal medulla, . Which of the following is the first product of tryptophan metabolism? a. Bradykinin b. Xantheurenic acid Leucotriene 4. Kynurenine ‘Tryptophan as a biochemical precursor: * Serotonin (a neurotransmitter), synthesized via trypto- phan hydroxylase. Serotonin, in tum, can be converted to melatonin (a neurchormone), via N-acetyltrans- ferase and 5-hydroxyindole-O-methyltransferase activities + Niacinis synthesized from tryptophan viakynurenine and quinolic acids as key biosynthetic intermediates. * Auxin (a phytohormone) when sieve tube elements, undergo apoptosis tryptophan is converted to auxins. |. Which of the following substrate delivers amino group to form urea? a. Omithine b. Arginine Aspartate 4. Alanine Urea cycle * Theurea cycle consists of five reactions: two mitochon- drial and three cytosolic, ‘+ The cycle converts two amino groups, one from NH4+ and one from Aspartate, and a carbon atom from HCO3-, to the relatively nontoxic excretion product urea at the cost of four “high-energy” phosphate bonds (ATP hydrolyzed to2 ADP and one AMP), + Omithine is the carrier of these carbon and nitrogen atoms. . In urea cycle, hydrolysis occurs during: a. Formation of ornithine b. Formation of arginine Formation of citrulline d. Formation of fumarate Omithine is formed by hydrolysis of arginine, reaction being catalyzed by arginase. Which of the following is FALSE regarding Seleno- gysteine? fa. Itis taken as 21st amino acid b. Coded by UGA c. Formed by cysteine and methionine ._ Associated with glutathione peroxidase Scanned with CamScanner 149 .(eimai! era Selenocysteine (abbreviated as Sec or U, in older Publications also as Se-Cys) * Iti the 2ist proteinogenic amino acid + Itacts asa building block of selenoproteins + Selenocysteine is a cysteiene analogue with a seleni- um-containing selenol group in place of the sulfur- containing thiol group. It is present in several enzymes Glutathione peroxidase, Tetra-iodo-thyronine 5’ deiodinases, Thioredoxin reductase, Formate dehydrogenase, Glycine reductase, Selenophosphate synthetase I, Methionine-R-sulfoxide reductase B1 (SEPX1) 67. Nitric oxide is derived from which of the following, amino acid? a. Lysine Aspartate Nitric Oxide/NO Arginine isa substrate for the production of NO ‘The enzyme NO synthase cleaves the nitrogen from the guanidine group of arginine to form NO This reaction requires NADPH, FMN, FAD, heme and tetrahydrobiopterin 68. What is the site for protein synthesis? a. Golgi body b. Granular endoplasmic reticulum ¢ Agranular endoplasmic reticulum d. Mitochondria A large portion of the endoplasmic reticulum is studded with ribosomes to give a granular appearance which is referred as rough endoplasmic reticulum. Ribosomes are the factories of protein biosynthesis 2. Which of the following provides stability to collagen? b. Tryptophan dd. Learginine a. Tyrosine b. Proline © Alanine d. Methionine Proline and hydroxylproline are present in large quantities (about 100 residues each) in collagen and these two amino acids confer rigidity to the collagen molecule. 70. Which of the following protein structures NOT affected if protein is denatured? a. Primary b. Tertiary ©. Secondary d. Quaternary Protein structure + Primary structure, such as the sequence of amino acids held together by covalent peptide bonds, is not disrupted by denaturation fe |. Carnitine is made fro 7. Catlysine and leucine _b. Lysine and methionine 2 Tacine and isoleucine d. Arginine and methioriny Carnitine ound otis a quaternary ammonium compound biosynthy ea dain theamino sc Iysiveand methionine Teas required for the transport of fatty acils from th we redeipraneousspace inthe mitochon, ioth mitochondrial matrix during the breakdown of lipids {{ats) for the generation of metabolic energy 72. Which of the following amino acid have some niacin sparing action? . a. Tryptophan b. Cysteine Methionine d. Tyrosine ‘Tryptophan can replace niacin to an extent of 10% for th oyrltenis of coenzymes. Therefore, both niacin and tryptophan have to be invariably provided in the diet 73. Which of the following vitamin is synthesized from tryptophan? 2 Vitamin 82 Vitamin Bt ©. Vitamin B3 Vitamin Bé 7, Niacin of nicotinic acid is also known as pellagra preventive (PP) factor of Goldberg. The coenzymes of niacin (NAD# and NADP+) can be synthesized by the essential amino acid , tryptophan Niacin deficioncy: (A) shows early signs: (8) depicts advanced skin lesions Amino acids below isoelectric pH exists as: a. Anion b. Zwitter ion © Cation, d. Dipolar Isoelectric poinvlEP * It is the pH at which a particular molecule carries no Standard nomenclature of isoelectric point is pHi. although pl is also commonly seen ‘The net charge on the molecule is affected by pH of its surrounding environment and can become mote positively or negatively charged due to the gain oF loss, respectively, of protons (H+). 5. Cystinuria is associated with is i ction of all EXCEPT: aiken la a. Lysine b. Cysteine ¢ Omithine d, Aspartate Cystinuria * Itis caused by mutations in the SLC3AI and SLC7AY genes. * These genes encode two parts of a transporter prot that ismade primarily inte kudnwys Scanned with CamScanner