Name: Biol 1610 Class 25 Worksheet Summarize what we covered in lecture today by filling in these pathways. Include the pathway names, input, output and intermediates. 1. ©©©©©© G3P P=c © ©©©—P G ©©© 4 Carbon 4 Carbon ATP 6 C. CITRATE 3. 2. 5 Carbon UNID 4 Carbon CCC acetate ။ (cIC) CoA To u CoA
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- v 11 v A A Aa v AaBbCcDdEe AaBbCcDc AaBbCcDdE AaBb( AaBbCcDdEe Styles Pane DE U v ab x, x A 2v A v 田。 No Spacing Heading 1 Normal Heading 2 Title Question 1: Compare and contrast the different metabolic pathways used by cells to generate ATP, illustrating your answer with a suitable table or diagram. Include in your answer discussion of the metabolic adaptations that occur in cells as they respond to changing internal and external environmental conditions.AA View Tell me Convert to SmartArt W- Picture Shapes - Text Box Arrange Quick d Tue Dec 6 3:13 PM ♫ Share Design Qsn 2 (a) A pathway consists of 6 enzymes (p, q, r, s, t, u) that convert substrate J to product X at a rate of 10 moles/hour. If enzyme q is increased from 5 mmoles to 35 mmoles the amount of product X increases to 20.5 moles/hour. What is the flux control coefficient for enzyme q (C¹)?Part 1: Draw the following metabolic pathways and identify different types of organic reactionmechanisms. Make sure to draw the structures of each biomolecule included in the pathway.1. Catabolism of triacylglycerols- beta-oxidation pathway2. Biosynthesis of fatty acids from Acetyl CoA3. Glycolysis (from glucose to two molecules of pyruvate)4. Conversion of Pyruvate to Acetyl CoA5.Citric acid cycle6. Gluconeogenesis pathway (pyruvate to glucose) Part 2: On your drawing, identify at most 5 organic reactions in each metabolic pathway.
- A. Identify different types of organic reaction mechanims in the following metabolic pathways.4. Conversion of Pyruvate to Acetyl CoA5.Citric acid cycle6. Gluconeogensis pathway (pyruvate to glucose) B. Identify at most 5 organic reactions for each metabolic pathway.Name: Sincere Frias Date: (0/2/2od0 Period Ced th nzy ck. Enzyme Models & Factors Affecting Enzyme Action PART I – Lock and Key Model st In this part you will construct models of enzymes. Remove the last page and cut all shapes out. 2. The different shapes will represent both enzymes and substrates. 3. Match up as many of the pieces as you can. 1. Questions 1. The enzyme maltase combines the substrates h ydrolysis + Starch molecule to produce the disaccharide maltose. 2. The enzyme ATPase combines the substrates_molecule and to produce the ATP (Adenosine TriPhospate). Iriglyceride 3. The enzyme lipase works on the substrate called 4. The enzyme phosphatase works on the substrate called 5. What is the relationship between the substrate and the enzyme?23 Which statement describes a disease state caused by altered protein structure? A silent mutation in hyaluronidase disnupts mucosal function OA slent mutation in arachidonic acid disrupts eicosanoid production O A missense mutation in heokinase disrupts glycolysis OA ronsense mation in ATP disrupts energy metabolsm
- What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55—62.)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%
- BIOMOLECULES Please answer the questions properly. - Multiple choice Qyestion 1: If a cell has an adequate supply of adenine nucleotides but requires more guanine nucleotides for protein synthesis: 1. Glutamine-PRPP amidotransferase will not be fully inhibited. 2. AMP will be a feedback inhibitor of the condensation of IMP with aspartate. 3. ATP will stimulate the production of GMP from IMP. 4. ATP will inhibit nucleoside diphosphate reductase. А. 1, 2, and 3 В. 2 and 4 С. 1, 2, 3, and 4 D. 1 and 3Answer the ff. questions: 1. To which class does each enzyme belong? Explain your answers. a.) pyruvate decarboxylase b.) alanine aminotransferase c.) alcohol dehydrogenase d.) hexokinase 2. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 3. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?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?