Exam2_key - C485 Exam 11 Fall ‘10 Name Legible please! Do...

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Unformatted text preview: C485 Exam 11 Fall ‘10 Name Legible please! Do not use acronyms. Use structures whenever they are asked for, or appropriate. Your explanations should be brief. Overly lengthy answers with irrelevant or erroneous material will receive deductions. GOOD LUCK 1. (33 Pts total) Please answer the following questions about glycogen metabolism. Use chemical structures where indicated. I , e V art-«era r a) 4 pts Draw the structure of the two different types ofiglycosidic linkages found in glycogenwtfi «Mo , 6% \n a ’01 L Pom-ts ~tw ca «NW __ l‘ .o tamflé‘wi b) 6 pts There are three chemical reactions required to degrade glycogen. Using @d explanations show what these are. \K _ W 0 @D Q-‘CIA ‘ l , D I l/ 0 fi 9 W I M /“9 Wri§ «a i” 13‘,” meebmam ’\ 0 R‘ 0‘ 4'1th 6m,”wa @ ooooowofi (D +C—Lbk ‘ C3) :1 poms *qu wot/x Vwbmm .. ~55 09 ere “Ham/m am qm P‘ to W mum/cm c) 5 pts Place the following steps of the reaction cascade of glycogen metabolism in the proper order: l poll/CC «for arid/i. a) activation of protein kinase A b) formation of cyclic AMP by adenylate cyclase c) phosphorylation of phosphorylase b d) hormone binding to target cell receptors e) phosphorylation of glycogen synthase a and phosphorylase kinase first ( i b 0\ Q‘ C“ last d) 8pts Using structures and explanations, describe the steps involved in the synthesis of glycogen via the Leloir pathway. M (04 ‘L < " \o twbS -— w u 9” . _ no 0,, 4. WP Walla-wme (WWI/L pan/UV erg ‘ M (W. “’5 2:1“ 47kg Gitgr-S’ym L e. Ghaoogcn'm flan “ht—Aw?“ éh’wy/mm ~OOOOUCDOO-ou W 9" B a ‘ i? f 7W Marisol (0606000 e) 5 pts Place the following steps of the insulin signaling cascade in the proper order: 21) Binding of phosphoinositide 3-kinase to SH2 domain i POI Vfi: “gov am M b) hormone binding and receptor dimerization c) phosphorylation of Akt by PDKl (PlP3-dependent protein kinase) (1) phosphorylation of IRS—l e) receptor autophosphorylation first b ‘2 é? 0\ C last t) 5 pts What is meant by reciprocal regulation? Give an exam le associated with glycogen metabolism. 3 poi/{+5 2 PD.\ ‘ \S Pm‘i‘flin (CIM‘VL/Pr adieu/in; [Mgplufijimz ILJM\ U/i/th/QA afii’wji’t) pMSPMMCX-‘xfl M Liter 3WW Ogcé QQWJynJ’iAA/VQ which “RU/V15 pmi'cin bkmA‘i‘M"; ‘ Whgls raw/Q @uW aLLlAXI u/Ltwé‘f/‘O sawsJL \fpwmicwafi Jurns oflri‘WPU/{Mrfi pie-n mirhwWy do. i‘hvatva on We romaine}. try WSW gr; . (30pts total) a) 10 pts Draw a mechanism for the conversion of methylmalonyl CoA into succinyl CoA. If there is a cofactor involved, you must indicate a basic idea of the structure of the cofactor and its involvement in the chemistry. 2’12??? (3 *9, ggahzlkfl‘saa 1 o. b) 10 pts Draw a mechanism for the conversion shown below. You may adjust rotonation states between steps so as to shorten your mechanistic scheme. If there is a cofactor involved, you must indicate a basic idea of the structure of the cofactor and its involvement in thechemistry. c) 10 pts Draw a mechanism for the reaction catalyzed by AcetleoA carboxylase. If /\ there is a cofactor involved, you must indicate a basic idea of the structure of the cofactor and its involvement in the chemistry. 0 vi 0 U at s Q 5‘ f ' x”? o v x“ t1 3‘ fit (A: 1- U i , U/ika rw/gr?.: O ADl 0% Hbgi¢m «Aye—Vflfl‘) w a; fig) /M;Uj-~_g y i “‘ I f1 "1) ‘ “)5 L” ‘ ‘ r, u /’ xx *5 (it rt J; ' HAM r r5 V :8 ii” ‘9‘ fl we Kf/ ‘N H t 2”“??pr \5: 558* W ‘ cw mam “‘4 W t. a M 5;» \WW \ ("K N 3. 15 Please an‘SWer the following short questions (4 pts each) a) What are the two major seureeS reducing power required for fatty acid synthesis? CLé-“jm s-ng (Mall: evile [2) b) How is pyrophosphatase involtyed in the activation of fatty acids for beta oxidation? it; 4— ’rT” we Al°”l"°* w: ~ A $~ 1'5, pampmflm/g grim mph )E l' h‘ l f " 'Zl’i‘rbt 'd' ff 'd c Xp aint e invo vement o carnitine 1n t e e a oxr ation o ‘ atty acr s. i 63.4 o T M /‘ C9 {-mn REM» + ‘57-; rim WWW eel,” 9243‘s a r w/ aim“ . 4?pr (itth 6 H5414 W”, W“ mid/$11” WM, *filwwwfi “"3 E:th d) What two properties Snake triacylglycerols more efficient than glycogen for e storage ' - f 2? > 7, ‘ \E‘Ctbirgrfiwwgw, «Jim/AA W 9MW2’J‘ Mam Wig/3mm WWW lip/CS L) 3-2,me Mona, Whaloto. PbfitflLo-«H. WL C/j Mum 4. 8 pts Please list four ways in which fatty acid biosynthesis is different than simply the reverse of beta oxidation. 2 pol n+5 +0» all Muir‘s/.3 in M pol», I3) Utsu M91)?» MSW 4 NM)” 6"”) M SsVCfl a “’t“ °"‘ “WWW gum ‘3 “Mufti MN: 15%“. I'n wbflm M. (‘9 35% Links /‘ m V WL’WJCO’Q‘ WM AaCofl \ pelt/rt tweed/t 00 V V W 4. (7 pts) Match the items in the left hand column with the correct item(s) from the right hand column. (Items in the right hand column may be used more than once.) AMP I Insulin 3 Palmitoyl CoA / l) downregulates synthesis of malonyl CoA 2) required cofactor for synthesis of malonyl CoA 3) stimulates synthesis of malonyl CoA Citrate 3 4) is part of the acyl carrier protein Pantetheine 7' 5) stimulates production of CAMP CAMP l Biotin g 6) essential cofactor for transamination reactions 7) released by the pancreas to catalyze peptide bond hydrolysis 5. (7 Pts) a) How many enzyme activities are required for attachment of ubiquitin to target proteins? b) Draw the attachment site between ubiquitin and proteins that are targeted for degradation. (You must show enough chemical structure so the nature of the bond and the relevant residues involved in the bond can be identified.) (4}) ti) AL”; Ta 6W Lipch 6.) (7 pts) a) 4 pts The two nitrogen atoms in urea are derived from amino acids. Which amino acids are these? b) 3pts What is the carbon byproduct of the urea cycle and how is this metabolized? 4“ A) Show lisp @47qu Moe/l2; ojoLQih‘iePW 3W3 7. extra credit (8 Pts) Calculate the approximate yield in ATP molecules of the complete oxidation of the C10 fatty acid shown below. (Show how you arrive at this number.) WW0 “‘9‘ 97p {jam}; oQngfiw g Agog 7. 50 ATP ll—lwtmg a; p oimtul-nin : tr NfiDH’ XL? :(oi‘ér'l'lf‘3 3 m H1 gawk“ «MbkbamobX 152%)” 5154.11? 4.9:? —2. f: fi-Tf «A 8. extra credit (8 pts) Nitrogen excretion via the urea cycle is an energetically costly process. Consider the processing of the amino acid shown below. How many ATP equivalents are used to process this amino acid via the urea cycle? How many ATP equivalents are obtained from the carbon skeleton of the amino acid? What is the net production of ATP from this molecule? 0 0 $3 Scat: 7 1019719 T‘A’ 0"" La .3 0’ N“ 73% 4/9, H T “W m M» J NH; 2.! ATP . LLQ '+ ATP WWW; lo gawk URéfiCg ” Nfibfl\ 85 ,errf’ M‘ LLH7(P(w2n:vE W boa-2.3” “Lt”: note cm {3% all} «M, 2‘05 #1“ F ...
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Exam2_key - C485 Exam 11 Fall ‘10 Name Legible please! Do...

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