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4033q2whitekeysum11

4033q2whitekeysum11 - BCH 4033 Summer 2011 Namezw Quiz#2...

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Unformatted text preview: BCH 4033 Summer 2011 Namezw Quiz #2 N—number: knew 2 5/”? Given that 128 ug of pure enzerQOO) converts 195 nmol SAP/min. What is the enzyme’s w turnover number? What is the time per turnover in seconds? 4, W Q I p W S w i Z 8 ['@ g W (I; {Q a éavka’g } a ég gift}? ‘ . new; Mk wee? gaggle {like “W'isrjlm t Mir TN. = Olaleg min"; Time per tfirnover= @ 1 gm? ec . ' h wté r. {Q j“ ’6'" V Wm.“ Define turnover number mathematically usmg Vmax and a speCific rate constant.W§ééfi-i r The molecule below affects themkinetic parameéirs of what kind ofi enzyme? a”? Mm: if / “r a W flax w" flirt/33% ma w v, obi NHz-CHz—CHZ- Hg-Efl‘lz—CH2—NH2—CH2-CH2—NH2 it t” “t ' “~ t EWMQgW .5 . gt} f7 62,63? w- J p ,r ,. m 1 W l W N l t“’¢-\~tr’u“€tzv‘ r 3'! ‘W‘iif‘f.’ tit'dwfie wig» “a; é 2m Ark; gay/Ha Ml?” i may 52%” ”; a. What term would best describe or identifymthis molecule? tree mirage VL‘t Wt [rut Z: #5:; m /« 9N b. Write the rate law for an enzyme inhibited by this molecule? W,“ f @1723 u [f j W 0. Draw a structure or reaction indicating the mechanism of how this moleci‘ile Effects the enz' me. Ve’fiwfimt; mé’éwtt; 2 5‘ n gm iota: % 69W: fig; x \ k A ‘ a, WWW”,- w a W W55“ “1 firm; v fig“ étw WW getting W IIi s‘fxfiiefi “new ‘3 I l mama" & r, it? ' autism; XL. Mama. An enzyme has a Km of 0.75 nM and a maximal velocity of 950 umoles/min. What is the substrate é: concentration that would give a rate of 415 umoles SaP/min? . C V?” ’ W5” ‘1‘ W’Sj ‘ Ellery"? 410110: 43mm? it,me tWCKZl / WW twins? ) j a. Name this monosaccharide as specifically as possible (use D— or L— in your answer). @M63r u .... 2:,» b. Draw the sugar above in Hawc‘iigfi1 projection as a B-D-sugar (use curved arrows on the Fischer projection to show how the ring is formed). BCH 4033. Quiz#2, Summer 2011 WW liar/g 2 6. given the following rate information, answer the following questions. Estimate Km, Km), Vmax & Vmax’l. // $5: [S] V0(mM/min) V0 (Inhibitor present [4.5mM], mM/min) 2.5x10': 210 26 r 4.0 x 10' 300 33 EM 1.2 x 10'5 525 66 2.0 x 10'5 712 89 4.0 x 10*: 960 120 2.0 X 10' 1042 130 M“ /_ ....... 1.0 x 10'2 @ 1050 132 kit: .. 3.42 a 5;“ W l «A M ,, Km=l\‘ MD M; vm= lawns Km 1J3?“ ; yum]: (2% MM Ma W "WM ‘ M M a. What kind of inhibition is represented in the table b. Find the K1 for the inhibitor. 2‘ 7 / (2:6 aria a6: $45. 0. Sketch a general Lineweaver-Burk plot for this type of inhibition. Indicate a line fer no inhibitor and V a line for inhibitor added. (Label points where K,m,Vmax, K.m,1& Vmam could be determined.) L9 MA a?” (13%»; » 43”?) fi é. m rmWwwwfinmamsmamgm “A W lme £5 E ‘7\ For oxy-Hb versus deoxy—Hb answer the following questions. (Circle the answer.) a. Defined as the relaxed state (R—state). flaky-lib r Deoxy—Hb or Neither or Both 2+ - - b. Fe 1S above the plane of the heme. Oxy-Hb ow or Neither or Both c. Does bind diphosphoglycerate. Oxy—Hb Neither or Both d. Has the distal His fixed by salt bridges. Oxy-Hb or’xm .or Neither or Both e. Has a binding site for a sticky patch residue. Oxy-Hb or Deoxy—Hb or Neither 0&2} ‘8\ General base catalysis is one of the mechanisms an enzyme may use to speed up a reaction. .., i g a. What must happe during the reaction in order for general base catalysis to operate? 9 , t m y‘ ‘9’}; f ,‘rxvflva Wfiwrjgéfigw Shieé 6‘3“ KigaazBQ mg. l b. What is an example of an enzyme that uses general base catalysis? d (we; mm}? 3 {Arm ,2 l c. What is the general base for the enzyme listed in part (b)? if 2, d. Draw a cartoon type reaction for an enzyme indicating how the general base functions. w é—élflamd lam ta. fl L \é’} f M ‘ I D CVVWW; «at [:2 fim R l ‘ W \Jma tr be tag f ., a, (1..., , ,' , r I W m biker? mm was.” X ...
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