An enzyme catalyzes He veaction AZB, The en&yme is present at a Cencentration of 2nl, an Vmax s 22 The "km fer Substrate A is 12mkl A) Calculate He initial rate (Vo),ulen the subtrate cancento is (em
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- Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is — 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37°C.
- PTP1B Substrate kcat Km. kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEP YLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 + 0.22 0.53 + 0.02 34.7 + 0.25 52.7 + 0.7 0.066 + 0.001 ) The units for kcat/KM in the above are given according to standard scientific notation. On this (d) ( basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?Comment on Figure 2a and Figure 2b regarding stabilization of the transition state and destabilization of ES complex during catalysis. (b) AG AG EX EX E+S E+P ES EP AG AG,+ AG- TAS ES EP Figure 2PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
- Catalane in un enzyme that speeds up the decomposition ot hydrogen peroxide H0) to waler and axvgen. Students conducted two investigationa to determine the ideal conditions for the function of catalane. One wetigation compared catalase activity at diferent values of pH. The other imvestigation compared catalane activity al diferent temperatures. Enayme Activity ve pH Enzyme Aetivity vs Temperature Teate C) According to the data in the graphs, which pH and temperature combination provides the BEST conditions for catalase to tunction? Anury lag aDiazepam is converted in vivo to an active metabolite Oxazepam. Explain metabolic transfomation of diazepam to oxazepam. (Provide names of enzymes involved in this transformation. Drawings of structures ofintemediate metabolites is NOT required)Metabolism of Lipids (R - PowerPoint 动画 EndNote XB < lipid Officel 开始 入 Qit a A a E 國 园 食 @ 圈 文档优化智能號 四G 登录 发送到微字体一色彩的一段统一三地折西西中西虚化图形图 機板 主题板 色彩選密表数密表图标 图片 PPTRS Office em 余源余源Live 編入素材 AITR 37 The peton patwyy Misban Rai 129 ATP Pay attention to : Shahzil Ch 129 how many ATPS are produced during Maryam Shanzadi: 129 ATP Amadooo: 129 ATP one molecule of palmitic acid! MuhammaCT Azhar: 129 ATP Go Live produced SAJJAD AHMAD: 7 FADH2, 7 NADH2, 8 40 108 Pay attention to : Say something veed during ... 单击此处添加备注 41 OT片第40张,共175张 02 E 小餐注 注 87%
- 1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex SeriosMaximum velocity of an enzyme-catalyzed reaction dolgomsH 7 T (8 a. Is determined from the slope of the line of product formation zouza11 901 ml,0,.201 over time for a particular substrate concentration. vx011(e b. Is determined from reaction rate late in the reaction d c. Is the rate where addition of more substrate does not cause a rate increase. SO 121 91 to ydinitis of zomit 001 vainitts d. Changes with increases in substrate concentration (II Which of the following is not an assumption in Michaelis Mentens kinetics?91 21 noi to 926 v basylsts noitsbyri riguard (SE a. [ES]~ constant b. [E] >> [S] 00 to fu291 6 26 9022it ni[*] 92691 T (EI c. [E] << [S]gnul art ni a.. Hq o bot Hq edt 1swol in d. [S] + [ES] [Sbaid atidinni slusslom 398-E 900 T antern anibnid yd 29tie gnibnidOn the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…
