33309 - Name Student ID # Chem 135 Final Exam Spring 2008...

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Unformatted text preview: Name Student ID # Chem 135 Final Exam Spring 2008 l. a) (5 points) Explain the basis for the following assertion. For efficient conversion of galactose to glucose— 1 phosphate, U DP—glucose need be present in catalytic amounts only. baffling 0g :l “Ls—w WKLGtQLa/mb WM” ‘ ' 142 DOES 5L» U 0 ?Ci JV“— fig‘fi- law?“ £62» «- l — pQDQyCLVi—erm Jewefilm mum. UT) P Ca «Ki/U” ) WV“ We,me in cum A. UD 1? m :60“ QMMmCL . H W\_ KN) P C»; M Q ‘ i 1 y . 3‘10“? C ‘3 N 3 U M E D A14,“ Xflxflx VWM {MM‘ U P ..... m AMVMJHMBQAK m vv?éi M x,me UK)?“ (Wow -‘ Li a WWW ‘ b) (5 _'nts) Althou h animals cannot s nthesize lucose from acet l CoA, if a rat is Pa g y g y fed ‘C-labeled acetate, some of the label will appear in the glycogen extracted from its muscles. Explain how this is possible. :5? “T (MA... NET “VH2: Q N E'3 L‘Gfi Mr “M91 C ‘92. WV” mega» MA two“; WWM‘ML" m . Elm.an if“; ~Qafiw§54sa£stnfi~ awxam’h’ Amalgam WMWW” ) Wravj‘gfim 3&3 Mi" {Jev’ir‘J’J-m ' 3"?" 1m“? CMX‘WQMEL: megawatt taiuigeaiu Km“ GA A; august. \J Wag; C.» (:3 A [A flare. c’filmw‘mwtnmwtfiamu x’Latmemwm Ker We’ve? m I. w #3:" J ,m ,m "Mn 5 p m “V t \6‘” ,‘ V 3 " ‘1?“ A > aw whiémfimauk Ll: b F t ‘prL «\Mfimkflvwilfia «4.133.. wwtaflrfiwhfiw~w¢éwfi a. imam“ \ r ‘ F a, ,m: ,- x t tfkmfim uwvmmyx if) 4» gym Tier flax/Ax Lat P am ,mm®av Li {3:} 9;!) (,4; h c) (5 points) Stipulate the energy cost of converting two actetyl CoA molecules to 3—hydroxybutyrate in the liver, and then regenerating two acetyl CoA molecules from this compound in peripheral tissues. (Explain how you arrived at your answer.) i Liven: )1 C? 9 ‘ 593A 0 O 2. r 360A SCQA # Chi-XSH Hip CDASH o 0 NADH “AD 0“ 0 l PERH’HEKAL 0H 0 NM NADH 0 a g; - A O , . Tm; )K/‘Koo , I khan» “Moo; 7.55% ; Me 3 f Mk9, it : sum ; O 0 «5(0- 4:‘ ~ .~ A I“ _ w _ __ Ij\_fii ()0 of colxbtt s ‘ Th : u Mm ML _ ——K~——$/—~————47 SCuA M 2» 5CoA twain/u. HYDRGM‘i‘bhfi o “a a 3“ . my ‘ an ‘ I fiu'w l a 0 A ~ / ., . W ' am PW" 52> Tth mw’bw («911‘ M“ WW f _ M m T C. A UWQQQ \AA. aquwimmt 19% «‘79 RQT’ p) ‘L‘d‘ry ‘ {hint/M , COST: tA‘TP Chem 135 Final Exam Spring 2008 ‘ Page 2 2. a) (7 points) Acetyl CoA labeled at C1 with 14C is added to a suspension of respiring mitochondria. Trace the fate of the labeled carbon by designating its location after i) one round and ii) two rounds of the TCA cycle. Briefly justify your choices of location. (33 Bus 9% 6COI\ + (5)?) 0 * CfiWOQ “'9' “"5" "-5- @DMMgC‘DA o o 4 . o . . i , «————> a A 0G) ( Se “0 «mug 19d. tyxmawnil kWh??? "‘WVCL‘a M” I‘m/Lg” walk) q s ‘ ' *“ ‘ a, o O O arm Achgui 369%.. Cs Maul; ,um. New 1 ' " ~ _ a r M . A “‘9' m} “*9 D é) Weave [rm—{r mmflyflwflflfl L ,3" MA; {3 {\A I Mam, O ww‘ kO‘fi‘Q" gm aw! X53“; ". eta/95a; -3 o Nor 0;: MM, W ) A? x; I (g) (3 C0,? 0 0 CA") W 3*. .3 l 0 ~\ H0 C“) , O H ., a 6:“) My 3*" re“ 1 Q I V; S A \J L V ‘ O C) "n NADQC NADH D U D ‘ Lch M39 « ~- ~» frfinl) ‘ A g; ’? IV ' . 15 tam ' la 4i wand?» (lam. MW L20}wa E g z} (jGJrk/Nrgqghm up * 0 V , 0 WA- C31 (amka‘SxALu/xg £9». AWm'MAL H EC}; ‘va‘wtk. xix/i’i Q’Vb’c’o‘fi’ b) (8 points) Identify and briefly discuss each of the mechanisms (both hormonal and allosteric) that prevent simultaneous fatty acid biosynthesis and fatty acid {5— oxidation in the same cell. "TV-(kg, MWA” E Wu‘wwkwm‘ (M “W (m by”): “LU” L‘VEQ G g“ LY§ rm cmwwuam CAM? CE) MWL'QA—K— “HM” WM“ ‘: ‘ ' E “W3 ‘ Y L k iNHrmeM 0% Wfle (WM («be 1 MM“ 39““ “DWWQQW Wk ACTNA‘TioN °§ gums/Wm M‘w‘flaJ—w‘ * sit W“ .uuzua aw» “AWW 9619‘“ ° "Limb Wheat-Wu... $3M. cmiwfi ‘0'“ 0% 0‘ MQ‘MQXW flw‘x “Mk KEAC‘T‘x \I’A'TES W—fiLC‘oA Lad-\wavdb/m. 9 (me ( 0c Wan/UL 93 GOA) Ac”: maxi-E5 Col-X umbm (flaky; target;le Wwaiim-ufll cx (Upb-(Xbpigi. ¥mesfi I \N H ‘3 tTS W “ FQMM a t) Cg XQ‘Q“ ,WfluLdflLAxiQfl fig flu; C‘QA kfi/(leA-Q- We) iMi—t IE 1T3 M 04.23}. C-QUNL’LLSLPL» 'mw.WJ. . 1 a \ , ‘ flu. fig max 8.43% MwiiJA—u (but. arm/fiducka W“ Wu- ;W,_ a; ' , Meta» 19¢). L3.“ {‘5‘ DU)“ ‘3. 1 34k kwi'W‘r‘im analluga. Waiuwmmzji, Q, A 2W6. W I {5 . (Agavwvei. My W Mug M1-WLVW(\-m Wat Mi. LQJMLAA : wax r» c . {A ‘14:». (Wt/\Wd» a Chem 135 Final Exam Spring 2008 Page 3 3. a) (8 points) The adenine nucleotide translocase and the pyruvate/H+ symporter import ADP and Pi into the mitochondrial matrix and export ATP to the cytosol. Stipulate how each of these effect the electrochemical proton gradient across the inner membrane, and explore the consequences of these effects on the number of protons that have to be transported C to M in order to energize the synthesis of cytosolic ATP from cytosolic ADP and Pi. C. M 4 a M ATP < R 4.5 6) AW m H g TRANSLocASE SYM?O\1TE$L<L \ ' I » A 2.433%» . «' “gun-xvii”. ck E) (Wag)— r; Mike-g may) ,mtqwnfix‘. (5-3, m (um h “if? Til/w. at,qu AD ? mm Pt; ‘Wvdk were Mt‘m‘fit ATP Mk “"WWt‘M’W‘w‘ h‘fi ‘m Cm“? M ,L 03 m HE). flair/tea, twig/amt)» m ATP ( 5‘" TH E M ATRV‘ i) M)” t I ‘ e v g C ,LxMU-rfigMbaimdn $2M} erW W “31L 6% TH'tLe e H 63 C M , W WWWM‘W‘ 6% L‘VTDDBM AT? swam CYT090L3C Abram/cat PL .W, W M 133% (meeg 1:092 H 42-Jqu tKQxL C. W " 1e» m 5"\ W 753$ mcifithmffiuqfi wwvvubb vmwwcm » b) (7p0ims) An iron—sulfur (FeS) protein in Complex lll reduces cytochrome c The half reactions and corresponding EO' values are listed below. Write a balanced equation for the reduction, calculate the standard free energy change for the reaction, and explain how it is possible for this transformation to be spontaneous under physiological conditions. 1. __Eo'.£V)__ FeS(ox) + e“ ——> Pegged) 0.280 Cyt C1(F€+3) + e“ ————> Cyt 01(Fe+2) "FeSUe‘flfi— ogLCJFe®i ~——-—————-—3> res-(ox) + nan. (RE?) AE° ":2 o.2\5v- ot'zeov 2 no.0e5v I y N ‘ AC0 = * WPAE" = w (tltaequTmfl‘lbDfiw/O fiW’YW WWVW 52.0?) fink. AC4 (VW’X AQQ‘E) .Tlm' 0% 5Q chalet/can (B'vx ‘Ifixuc C To. W. ta Mica W (W3... sow We?“ M brat“. file We Lu.» W 0% cg, We 0% CsuvLE‘o J23 JWQMCB» I J’s/a“ firth e28 CE ,Lm th Wm Luwmc, ALWW ‘ Chem 135 Final Exam Spring 2008 Page 4 4. a) (5 points) Explain why a cell preparation containing all the enzymes required for the fi~oxidation pathway is unable to generate ATP upon the addition of a fatty acid unless a small amount of ATP is also provided along with the substrate. $30“? in» may;wa 110x M ACE\Vi>~T\Di-l 9-? WCni’x _ m1; Sun. flu, 73M filed ‘ floaf» um hecifli—vlbkm war m maxihvfik ~ WWW» « 0 AT? AM? 0 o RAGE} “%—M “Jksom‘cwx -i a.» fixed)». (WW‘L’K) COASH it”; t xvi/a .Mu-ba. W,e~wgm 329» m cumvcrcflwm rw‘kbmio—tfl ' ~ ~ ~ w» b) points) A fasting animal is fed palmitic acid (a 16:0 fatty acid) that has a C-labeled carboxyl group. Afterlallowing sufficient time for B—oxidation and fatty acid resynthesis, what is the C—labeling pattern in the animal’s palmitate residue? (Explain) (5 Meow [l-~MC1 (la/£339. CAR 032 753d. C ('beCo/x‘) . MU (La/\EL'U'VV JVMW «fig. ” m (mt ODD NUMBERED 13¢ » “Maui i “c - MM ; 9 wk pct? AD? 9 =)ni‘\50°’\)flcz 0 o o i , i‘ «a ,L ‘ . “ “t ' ’- “‘5 SC‘GA ——%é‘——) C K/*\5Lflf\ .M 4+ ,7 00 CD 2, P I . . 5. a) b (5 points) Descrlbe how the reverSIble glutamate dehydrogenase catalyzed reaction can contribute to amino acid biosynthesis as well as serve as an anaplerotic reaction. Q N p“ D Fri/k S) H G a} a “l. , x i ‘ l, ‘3 r: (:3 t7} xv/W 0 ttfig’umv/ mm .. N M a ._ (yaw HZD N M at” “a, a; ‘13 TL. W vaotxedn cwbwazkéu. Asa. WVLuv‘éwiscA. aim-1%” WK Kick : P at A magmas beam ,2” list“ at. ewe. l’i‘t Ni“ PLE; (LEV? NC» AWMAKWW » 1: W “tighfiv J‘i’w’é‘mm ed K'CR Wwartfilwcfe ,fimfi. athpvam { i b) (5 points) Production of the enzymes that catalyze the reactions of the urea Cycle increases or decreases according to the metabolic needs of the organism. Increased levels of these enzymes are associated with diets high in protein as well as with starvation! Explain this apparent paradox. Diana firefagfiv ~ \ . w A a... m is ,. ,, .vaw r~ ~' ' v- v P CL,C,‘&,« Ergw. “£257. Cay-3Q, N t \ (Lott. use a; m a, fiend; M» idea. .ng. Cit": cw U {a} gamma. I t % owl-£31» Wfikfiafia vmeefie xiii.» avg/mii’fi .‘s r w WMJA Xe... Anagram-gag “was, gmmhauaai W1 . mwflwmg W Wflgymt MueCLE fifififix my .24.: _ (a tea» a, . Us... Mr:— fiwm We firtdir‘ffltwfl M WWW Kiwi??? "Em-«Re; N raga. com, KARE A . 2% EfimTH Wi‘inefiww Q‘M"dt jflwa‘ WA" M mama N 1'1”?th «:4; ta 123w wxamido‘a Chem 135 Final Exam Spring 2008 Page 5 6. a) (7 points) Patients in shock experience decreased delivery of 02 to tissues, decreased activity of the pyruvate dehydrogenase (PDH) complex, and increased anaerobic metabolism. Excess pyruvate is converted to lactate which accumulates to cause lactic acidosis. Since 02 is neither a substrate or a product of the TCA cycle, why do low levels of 02 depress the activity of the PDH complex? Ammdgtt 0.; Lu; W a mum Max M cgm'mpi again} A‘JL $.43- MLW {Lam 129cc. AWQA WWW 0% "IBM, NA 0 H (“EAL/vut M “41% M m h M 02—41). Wnugl Wilma.“ avg MA‘DH WWW ELEVATED MM W\ ogNAD A ’ « " h ’ ' 'r ' DECLINES . Hugh “Maw/[MAW] ) Wm Max/amt. 1% PM LWLAL Ck) PRODU QT tNt—HBiTtoN W bl NP‘DH 19¢ _ gill?!»in 4 Cim‘ix _ T45; A M’ I twwmxwam ' AAA. glytrtm/cmi‘wkiwwm l Mum/wk 3W» flaw. Mvwmmb cam Vi) i-t mm»... N A i?) H i > b) (8 points) Acetyl CoA inhibits dihydrolipoyl transacetylase (E2 of the PDH complex) but activates the PDH kinase component of the complex. Explain how these opposing effects on enzyme activity are consistent with the overall regulation of the PDH complex. Ame axamam (sq) M H Q t 20»: 2.1, a} mm 4W " l W amt/«Jinx. =g> BOTH EFFECTS 330ng m mHIBtTum. iantfiWWmclaW“" egotamgtcspx W mm TCA owwonnmm _ mew M fiamwwme ATva M Wm M]. W W Wag WWW Qua INHIBK‘T’ED. ‘ Chem 135 ‘0'} m1“: 3’ m I {K :3 Final Exam Spring 2008 Page 6 7. (20 points) Match the letter designations of the structures/symbols/terms with the descriptor statements provided below. HO » mg HO 8 I? 0% N HO O-r-e-t 9 o 9 o ACP HO OH (A) (B) HMG CoA Reductase 9 CU SCOA compartmentalizati on UCPI (D) (E) (F) (G) H 903 malatc—aspartate shuttle 9 O _ 09 i (H) (I) (I) A mechanism for transferring cytosolic reducing equivalents into the mitochondrial matrix A substance that can be detected in the breath of severe diabetics in response to an overproduction of acetyl CoA. The portion of the polypeptide that serves as the substrate entry point in mammalian fatty acid synthase. A mitochondrial protein used to generate heat in response to a hormonal signal. A metabolite that inhibits the acyl carnitine carrier. A substrate of glycogen synthase. The active form of a medication given to patients suffering from hyperchoiesterolemia. A mechanism of metabolic regulation. An enzyme that is regulated primarily by the alteration of its rates of synthesis and degradation. A metabolite that shovvs an increase in its cytosolic concentration when a cell makes a transition from catabolic ATP generation to anabolic ATP utilization. ...
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33309 - Name Student ID # Chem 135 Final Exam Spring 2008...

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