BIS102 Final F03 Key Doi

BIS102 Final F03 Key Doi - a» y/ {i \,L i K534 g: ‘z 6;...

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Unformatted text preview: a» y/ {i \,L i K534 g: ‘z 6; 55’ Biological Sciences 103 Name Section 1 Last, First MI Instructor: Roy H. Doi Final Examination December 10, 2003 Be sure to write your name and ID number on the Scantron sheet. Be sure to mark Test Form “B” on the Scantron sheet. Please mark the Scantron sheet carefully with a #2 pencil. There are 12 pages including this front page. Make sure all pages are present There are 50 questions. Each question has only one best/complete answer. Each question is worth 4 points. Be sure to turn in this exam along with your Scantron sheet. 1, _______________, ID# authorize the University to publicly distribute this graded exam (e. g. handed out in class or left in a bin for me to pick up). Honor Code: My signature below affirms that I wrote this exam in the spirit of the honor system of UC Davis. I neither received nor furnished any "help" during the exam, nor did I use any unauthorized references. Signature 1) The conversion of NH3 to NO3’is called: a. nitrogen fixation b. nitrate assimilation C. respiration d. biological nitrogen fixation Ca? nitrification 2) To reduce one mole of N 2 to two moles of NH3 requires __ electrons using the biological method and _ electrons using the non-biological (industrial) method. a. 6,8 b. 8,4 6.": 8,6 5‘ 6,4 6. 6,6 3) N02‘ is converted to NH3 by the enzyme: 9““3 . . (gynimte reductase . nitrate reductase c. hyponitrite reductase d. nitrosomonas e. ammonia reductase 4) The phosphoroclastic reaction produces three metabolites that are used during N2 fixation. These three metabolites are: a. C02, Hi ATP b. C02, Fdred, ATP (3. C0,,ded,H+ d. ‘Fdred, H+, ATP 6. ’ Fdred, C02, ATP 5) Which of the following is most sensitive to oxygen: a. DNR ‘12, DN FeMoco d. NH3 e. NO 6) When ATP binds to DNRred, its redox potential shifts from —O.25 volts to volts. a. —0.2 b. 0.4 c, ‘ 0.2 Q? -0.4 e. —0.45 7) One of the following statements is not true “The hypothetical intermediates during nitrogen fixation are diimide and hydrazine. (byOne ATP is hydrolyzed when two electrons are passed from DNRred to DN. c. FeMoCo is the co-factor for DN. d. The oxidation of pyruvate provides reducing power for nitrogen fixation. e. The main function of DNR is to pass electrons to DN. 8) The substrate and products for the acetic kinase reaction of the phosphoroclastic reactions are a. acetleoA, ADP, ATP, acetic acid b. acetylphosphate, Fdox, ATP, acetleoA cgacctylphosphate, Fdred, H+, acetic acid @.}cetylphosphate, ADP, ATP, acetic acid efacetleoA, ADP, ATP, acetic acid 9) The hydrolysis of acetyl—CoA releases more free energy than the hydrolysis of acetylphosphate a. True (inalse 10) The following enzymes are used to incorporate NH3 into amino acids by plants and microorganisms: is. _ a. glutmate synthase, glutamate dehydrogenase, glutamlne synthetase b. glu‘t‘fnate kinase, glutamate transaminase, glutamine synthetase c. glutmate synthase, glutamate transaminase, glutamine deaminase d. glutmate kinase, glutamate transaminase, glutamine transferase Gfiglutmate synthase, glutamate transaminase, glutamine synthetase 11) The conversion of the vitamin, pyridoxol to phyridoxal phosphate requires the following: 21. ATP, NAD+, pyridoxol kinase, pyridoxol phosphate dehydrogenase bimATP, FAD, pyridoxol synthetase, pyridoxol phosphate dehydrogenase CglATP, FAD, pyridoxol kinase, pyridoxol phosphate dehydrogenase . ATP, NAD+, pyridoxol kinase, pyridoxol phosphate acetylase e. ATP, FAD, pyridoxol transaminase, pyridoxol phosphate dehydrogenase 12) During the transaminase reaction, a transient form of the co—factor called is formed which transfers its group to an acceptor to form an of the acceptor. a. pyridoxal phosphate, Ot-kCtO acid, amino acid b. pyridoxamine phosphate, oz—keto acid, aldehyde Icifiyridoxamine phosphate, oc—keto acid, amino acid . pyridoxol phosphate, oz—keto acid, amino acid e. pyridoxamine phosphate, [S—keto acid, D—amino acid 13) Pyridoxal phosphate (PLP) is bound to the transaminase enzyme by a. uncharged groups of the PLP, hydrophobic groups of the transaminase protein, Schiff base formation b. hydrophobic groups of the PLP, charged groups of the transaminase protein, Schiff base formation cigcharged groups of the PLP, charged groups of the transaminase protein, amino bases @Eharged groups of the PLP, charged groups of the transaminase protein, Schiff base formation e. hydrophilic groups of the PLP, charged groups of the transaminase protein, acidic residues 14) The donor amino acid during the transaminase reaction displaces the group to form a which is formed by an interaction between a and an group. Ca/lysine, Schiff base, primary amine , aldehyde b. arginine, Schiff base, alcohol , aldehyde c. lysine, Schiff base, primary amine , alcohol (1. lysine, amide bond, primary amine , aldehyde e. arginine, Schiff base, primary amine , amide 15) During regulation of glutamine sythetase (GS) by covalent modification, the presence of high levels of ATP and a—ketoglutarate stimulate , which causes the formation of which interacts with which causes the of GS subunits and creates an GS. a. uridylyltransferase (UT), PH, adenyltransferase (AT), deadenylation, active b. uridylyltransferase (UT), PII—UMP, adenyltransferase (AT), adenylation, inactive uridyl releasing enzyme (UR), PH—UMP, adenyltransferase (AT), deadenylation, active d./uridylyltransferase (UT), PH—UMP, adenyltransferase (AT), deadenylation, active 6. uridylyltransferase (UT), PII, adenyltransferase (AT), deadenylation, inactive 16) The presence of high levels of glutamine causes formation and the of glutamine synthetase (GS) to form , the form of GS. {a\PII—UMP, adenylation , GS—AMP, inactive LIB/PH, adenylation , GS—AMP, inactive c. PII, adenylation , GS—AMP, active (1. PH, uridylation , GS, inactive e. PII-UMP, adenylation , GS, active 17) During cumulative end product inhibition of an enzyme, one of the following statements is true éfiaw product is a partial non—competitive inhibitor b. each product is a partial competitive inhibitor 0. each product is a partial uncompetitive inhibitor d. a product cannot inhibit the activity in the presence of another product e. 100% inhibition can be attained if all the end products are present at high levels 18) During cumulative end product inhibition, products D,E, and F inhibited the first enzyme of a biosynthetic pathway by 50%, 30% and 10%, respectively. If all three products are present in excess, the amount of activity remaining Will be a. 285% b. 68.5% c, 90.5% (5.315% ei’ 10.5% 19) The reaction carried out by ATP sulfurylase has a AG" 2 +50 kJ/mol. The reaction still occurs because it is coupled to the hydrolysis of and to the formation of and the expenditure of equivalents of ATPs during these coupled reactions. a. acetyl—CoA, adenosine—3’—phosphate-5’-phosphosulfate (PAPS),3 b. pyrophosphate, adenosine—S’-phosphosulfate , 2 pc. pyrophosphate, adenosine-3’-phosphate—5’—phosphosulfate (PAPS) , 2 @pyrophosphate, adenosine—3’—phosphate—5’-phosphosulfate (PAPS), 3 e. acetyl—CoA, adenosine-5’—phosphosulfate (PAPS), 3 20) The reduction of HSO3' to HSS requires electrons, NADPHs, and the enzyme a. b: 8, 3, sulfite reductase ‘6, 3, sulfite reductase c. 6, 3, sulfite dehydrogenase d. 6, 3, sulfate reductase e. 8 6, sulfite reductase S 21) Sulfur is found in the following compounds a, NAD, lipoic acid, biotin, thiamine, cysteine, methionine @‘COA, lipoic acid, biotin, pantotheine, cysteine, methionine c. CoA, ornithine, biotin, thiamine, cysteine, methionine d. CoA, lipoic acid, pyridoxol, thiamine, cysteine, methionine e. FAD lipoic acid, biotin, thiamine, cysteine, methionine 22) Serine, a precursor for synthesis of cysteine in plants and microorganisms , is at its group and then displaces the acetyl group with the release of CE? acetylated, hydroxyl , H23, acetate bf. phosphorylated, carboxyl , H28, acetate c. acetylated, hydroxyl , sulfate, CoASH d. acetylated, hydroxyl , sulfite, acetate e. phosphorylated, hydroxyl , HZS, acetate 23) In a mutant bacterium, cystathione accumulated and the bacterium required methionine for growth. The gene for the following enzyme contained the mutation: a. cystathione synthase I b. homocysteine transferase 7’” . Tr'v ‘ f L; cystathionase I 3 . cystathionase II e. cystathione synthetase II 24) Methionine is an essential amino acid for humans for the following reasons a. cystathionase II is missing b. homoserine is not synthesized ,ch‘the gene for aspartyl kinase is missing (EL/b, c e. a, b, c 25) The components of folic acid include a. glutamic acid; 2 amino, 4 hydroxy, 6 methyl pterin, o—amino benzoic acid flbk aspartic acid; 2 hydroxy, 4 amino, , 6 methyl pterin, p—amino benzoic acid Lgyglutamic acid; 2 amino, 4 hydroxy, 6 methyl pterin, p—amino benzoic acid . glutamic acid; 2 amino, 4 hydroxy, 8 methyl pterin, p-amino benzoic acid e. aspartic acid; 2 hydroxy, 4 amino, 6 methyl pterin, o—amino benzoic acid 26) Tetrahydrofolate is synthesized from folic acid by the action of and and the reduction of N 5, , and C7. a. tetrahydrofolate reductase, folate reductase, C6, N8 b. folate reductase, dihydrofolate reductase, C6, N10 c. folate reductase, tetrahydrofolate reductase, N8, C4 , folate dehydrogenase, dihydrofolate reductase, C6, N3 egdihydrofolate reductase, folate reductase , N8, C6 27) The lack of aspartyl kinase in humans leads to a dietary requirement of the following amino acids: a. lysine, methionine, aspartate, threonine b. isoleucine, methionine, aspartate, threonine rawaspartate, lysine, glutamine, methionine dyisoleucine, lysine, methionine, threonine e. lysine, aspartate, glutamine, threonine 28) The of the group of glutamic acid prevents and allows the synthesis of the amino acid which is a precursor of a. acetylation, carboxyl, ring closure, ornithine, arginine b. acetylation, amino, ring closure, ornithine, lysine Sixphosphorylation, amino, ring closure, citrulline, arginine d.‘acetylation, amino, ring closure, ornithine, arginine e? acidification, amino, ring closure, proline, arginine 29) The two groups of glutamic acid semialdehyde that can react spontaneously are ‘JL/‘J' a ‘carboxyl and amino groups (galdehyde and amino groups c. aldehyde and acetyl groups (1. amino and methylene groups e. amino and phosphate groups 30) The biochemical conversion of an acidic group to an alcohol group includes activation of the group by a , followed by to an and then another with the use of to form the alcohol group. a. aldehyde, dehydrogenase, reduction, aldehyde, oxdiation, NAD+ b. carboxyl, kinase, reduction, aldehyde, reduction, NADH + H+ c.»carboxyl, kinase, acetylation, aldehyde, reduction, NADPH + H+ (gearboxyl, kinase, reduction, aldehyde, reduction, NADPH + H+ . aldehyde, acetylation, oxidation, aldehyde, reduction, NADH + H+ 31) During a biosynthetic reaction, is usually used as the electron donor; during a kinase reaction is the phosphate donor; and during a synthetase reaction is involved as the phosphate donor; and during an adenylation reaction is the nucleotide donor. a. NADH + H, ATP, ATP, ATP b. NADPH + H: ATP, ATP, GTP c. NADH + H+, ATP, GTP, ATP d. NADPH + H+, ATP, GDP, ATP @NADPH + H+, ATP, ATP, ATP 32. The compound that can carry nitrogen readily from one part of an animal body to another is a. glutamic acid b”. serine @. I glutamine C aspartic acid e. proline 33) During degradation of ketogenic amino acids, the following compounds may be formed ("Eijsacetone acetyl-CoA, acetoacetate, 3-hydroxybutyrate . acetone, acetoacetate, acetic acid, butyrate c. butanol, acetoacetate, acetyl—CoA, 3-hydroxybutyrate d. acetone, acetoacetate, acetyl—CoA, formate e. butanol, acetyl—CoA, acetoacetate, 3—hydroxybutyrate 34) Amino acids can be converted into glucose, fatty acids, ketone bodies, hormones and purines. . I». L2: true b. false 35) The reason that argininosuccinate is a compound that bridges the TCA cycle and urea cycle is a. it contains an amino acid and its hydrolysis results in succinate and arginine production. contributes fumarate to the TCA cycle and arginine to the urea cycle. c. its hydrolysis directly yields fumarate and ornithine. d. it contributes succinate to the TCA cycle and ornithine to the urea cycle. e. it is a direct product of a TCA cycle intermediate and citrulline. 36) The two compounds that contribute nitrogen directly to the urea cycle are and The formation of one mole of urea from the precursors requires the expenditure of mo] equivalaents of ATP. Cay/aspartate, carbamylphosphate, 4 b. aspartate, carbamylphosphate, 3 c. fumarate, carbamylphosphate, 4 d. aspartate, acetylcarbamate, 3 e. fumarate, carbamylphosphate, 3 37) Carbomyl phosphate synthetase forms by condensing and and {he hydrolysis of . a. carbamylphosphate, NH}, H20, 2 ATP. b_,_ornithine, carbamylphosphate, H2O, NH3, 3 ATP. Gycarbamylphosphate, NH3, C02, 2ATP. d. ornithine, NH3, C02, ATP. ( e. carbamylphosphate, NH3, HZO,3ATP. 38) The mitochondria and cytosol play a part in the urea cycle, because is formed in part from ornithine in the , and and and urea are formed in the a. citrulline, cytosol, argininosuccinate, arginine, mitochondria @‘L‘,.citrulline, mitochondria, argininosuccinate, arginine, cytosol . carbamyl phosphae, mitochondria, argininosuccinate, arginine, cytosol d. argininosuccinate, mitochondria, citrulline, arginine, cytosol e. citrulline, cytosol, argininofumarate, arginine, mitochondria 39) An reaction furnishes the amino acid to the urea cycle when is removed for synthesis. The precursor to the amino acid that keeps the urea cycle going under these circumstances is a. anaplastic, ornithine, arginine, protein, aspartic acid b. anaplerotic, aspartate, arginine, protein, glutamic acid c. amphipathic, arrginine, ornithine, protein, glutamic acid ’fdkanaplerotic, ornithine, arginine, protein, aspartic acid be. anaplerotic, ornithine, arginine, protein, glutamic acid 40) The precursors for the nitrogen in the purine ring are , and ,,_a..glutamic acid, glycine, glutamine (biaspartic acid, glycine, glutamine c: aspartic acid, serine, glutamine d. serine, glycine, asparagine e. aspartic acid, glycine, asparagine 41) The first step in purine nucleotide synthesis is carried out by which forms from and a. amidophosphoribosyl transferase, ribosylamine, B—S—phosphoribosyl- l — pyrophosphate (PRPP), glutamine b. amidophosphoribosyl transferase, phosphoribosylamine, a—S—phosphoribosyl—l— 4 pyrophosphate (PRPP), asparagine Cfamidophosphoribosyl transferase, phosphoribosylamine, oc—S—phosphoribosyl-l— pyrophosphate (PRPP), glutamine d. phosphoribosyl transferase, phosphoribosylamine, (x-S—phosphoribosyl—l— pyrophosphate (PRPP), glutamine e. amidophosphoribosyl transferase, phosphoribosylamine, B-S-phosphoribosyl—l- pyrophosphate (PRPP), glutamine 42) The branchpoint in purine nucleotide synthesis occurs at the compound _ which is oxidized to __ and then converted __ with the use of ATP and to form __ a. inosinic acid (IMP), xanthylate (XMP), asparagine, guanylate (GMP) b. inosinic acid (IMP), xanthylate (XMP), asparagine, ade nylate (AMP) c. inosinic acid (IMP), adenylosuccinate , glutamine, guanylate (GMP) inosinic acid (IMP), xanthylate (XMP), glutamine, guanylate (AMP) (elinosinic acid (IMP), xanthylate (XMP), glutamine, guanylate (GMP) 43) In cooperative feedback inhibition Lab/the inhibition, when two end products are present, is greater than an additive effect b. the inhibition requires that both end products be present before any inhibition occurs c. the inhibition by each end product is a percentage of the remaining activity d. none of the above e. all of the above 44) In pyrimidine and purine nucleotide synthesis a. purine nucleotide synthesis is a branched while pyrimidine synthesis is a linear pathway b. the precursors are simpler for pyrimidine nucleotide biosynthesis c. the major point of regulation is at the first step of the biosynthetic pathways d. the formation of the deoxynucleoside diphosphates occurs at the level of ribonucleoside ragiphosphates Q all of the above l0 45) During the salvage pathways for nucleotides a. phosphoribosyl transferase transfers a ribose—S—phosphate to a purine or pyrimidine base. b. a nucleoside kinase adds a phosphate to a nucleoside to form a nucleoside monophosphate. c. a bacterial cell will turn off its pyrimidine biosynthetic pathway if it is provided with uridine in the medium. a and b era, b, and c 46) If a large amount of uridine is added to a bacterial growth medium, it would affect most directly a. the synthetic pathway for purine nucleotides b. the synthetic pathway for pyrimidine nucleotides C. the activity of aspartate transcarbamylase £1. a and c (e. b and c 47) In concerted feedback inhibition @?the inhibition requires that both end products be present before any inhibition occurs b. the inhibition, when two end products are present , is greater than an additive effect c. the inhibition by each end product is a percentage of the remaining activity d. a and b e. none of the above 48) Substrate level phosphorylation and oxidative phosphorylation are similar in the following way: u @ATP is the product b. Oxygen is required for both reactions to occur 0. A direct electron transport system is required (1. A high energy substrate is required e. all of the above 49) CoASH, lipoic acid, and phosphopantetheine have the following common property that make them useful in enzyme reactions a. they all contain sulfhydryl (-SH) groups b. they are relatively long molecules that allow them to react with active sites 9,. they are all derived from vitamins (fl/a and b e. ll 50) In a biochemical process, the energy released in an exergonic chemical reaction can be used to drive another reaction that is endergonic. The two coupled reactions must share an intermediate. a. false Kl: true Wishing you a Happy Holiday Season!!!!! 17. ...
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This note was uploaded on 10/22/2010 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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BIS102 Final F03 Key Doi - a» y/ {i \,L i K534 g: ‘z 6;...

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