sp05-1%20word%20problems%20key

sp05-1%20word%20problems%20key - Metabolic Biochemistry I...

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Unformatted text preview: Metabolic Biochemistry I BIBC 102 Midterm Exam / Spring 2005 I. (20 points) Fill in all of the enzyme catalyzed reactions which convert glycogen to lactate. Draw the correct structure for each intermediate molecule, showing the correct position of the hydrogen atoms at each carbon atom. Include the names or abbreviations of any other reactants and products (eg, ATP, ADP, Pi, NAD+, NADH, etc), and any required prosthetic groups (eg, biotin, TPP, etc). (NotezYou do _1_1__o_t_ need to give the correct name for each intermediate molecule or the correct name of the enzyme to receive full credit. Partial credit will, however, be given for the correct name of an intermediate structure if the structure itself is incorrect.) Glycogen (draWZ terminal sugar subunits 11: the polymer only) / c Haw .. ' -- _- r,.-----L\ | I l f. ' lactate (draw structure) II. (20 points) A. Given a mitochondrial extract with all of the enzymes and cofactors normally found inside mitochondria but lacking pyruvate dehyd rogenase completely, show how pyruvate, CO2, and acetyl CoA can be used to form succinate when succinate dehydrogenase is inhibited by malonate. (Assume there is I a no oxaloacetate initially present.) Draw the correct structure for each intermediate molecule, showing the correct position of the hydrogen atoms at each carbon atom. Include_th_e na_mes or abbreviations of any other cactants_and products (eg, ATP, ADP, Pi, NAD+, NADH, etc), and any required prosthetic groups (eg, biotin, r'PP, Iipoate', eth). .. NW“ _, u, for {initial . ‘ I- , 1r i? missed) ,o‘ cn,c_sc;1r+,- 1' ‘~‘ / 'u /’ t W“ 9 C- . ' Hg—c o; ' B. Show the path of 1“C la 4el in each molecule above starting with 14C label in the nethyl carbon of pyruvate( CH3-C(0)—C02-). ( I v --" I”. N 3 f/}_ . .I _. (‘4' I. "h J Lab“) .1 III. (3610mm) (2) Draw a diagram of the overview of proton and electron circuits in mitochondria starting with NADH in the matrix and ADP and Pi in the cytosol and ending with the reduction of oxygen to water and the formation of ATP (the diagram in the lecture handout will receive full credit). Label each - mplex and protein, identify matrix, intennembrane space, and inner membrane, and indicate the flow of protons and electrons. 0)) Indicate on this diagram the relevant electron carriers in each complex of electron tranSport (e.g., FeS, cytochrome a3, Cu, FMN, etc). 4 IV. (15 points) (A) In the space below please sketch the v versus [S] plot for an enzyme obeying Michaelis— Menten kinetics in the presence and absence of a campetitive inhibitor. Assume an inhibitor concentration of [I] = Ki. Please label lines, and indicate Vmax and Km for each plot. (B) In the SpaCQ‘W: 'FV 9-- Ccfifielé‘fl)? Vm, [SJ (5] +— lfi, (l l _ (I [s 5 —-~; leg-"sketch the v versus S plot for an enzyme which shows positive cooperativiry in substrate binding, in the presence and absence of an allosteric inhibitor. What form of the allosteric enzyme binds t e inhibitor better, the R state or the T state? PFK-l activity (G’s of Vim“) I—'——— .— {5) (C) The graph below shows the v versus [S] plot for phosphofructose kinase and its substrate ATP. Explain the shape of this curve. (Hint: consider the different sites on PF K to which ATP can bind). 100 “Cw/51,3 Puff-Ln o‘F Curt/£— Lia Ethfill-A’B I“ M; agents 4‘ S b.3012)? 1L4: flucwfl’ka 19”“; J} 4L, curve_ I}: 7" AM k {(A4 4/]:- fk‘r-C {w (147)” I} An) A/AafA/r-c nix/G935» of FPO 80 60 40 20 in! [ATP] a Vmoints) Acceptor control. In the following problem, you are given purified, intact mitochondria, an abundant source of matrix NADHa Oz, and phosphate. You are also given the following diagram: 1? _ 0: éolosm’ofiiw) f- ma/ 0 A. Please draw the lines expected for the time course of 0; consumption following the addition of 50 and 100 nmoles of ADP (you should plot the results of the two separate experiments as two lines emanating from point “a‘hon the graph). (Assume that there are 30umoles of 02 initially present). B. Does the rate of 02 consuniption differ in the two experiments? If so, by what factor does it differ? 1L; mJ-c o‘F 0:. Cwsfihfi‘ff af— wort/‘15} [+010 :3- ' z‘wzé:"'~-7 . At {:19 swarm; HP 3% C. What is the final number of ATP molecules produced from 50umoles of ADP at the point thatfurther 92—— eonsWow many O; molecules have beeneonsumed at this point? For full credfltz please show your calculations. _ I " '""' " _._s.._O./ufl§”{ I‘l‘o/J Tie/J [4/10, M7u,‘"_, M, 5.9.“: 4 (50):)110)(qfl’/197¢) [gym Hg.) safe {as _ mm. (Lax/v; 67 '4er Avnflwe. M yak/ow .2 Pun-70"! chit 47 fl“ '"Mu- "747441: f'aj-‘f/fiA-c'fi' _m.y {n .9117 7fl_..¢.3l_ul.:_ e “'3‘!ng _/ -'I '21.: 6273‘» “Am-$J-l) :9me ’0 fio/c'o- of: D. Why is the rate of 0; consumption essentially zero prior to the addition of ADP? ...
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sp05-1%20word%20problems%20key - Metabolic Biochemistry I...

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