ENZYME ACTIVITY
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- Comparing Glycolysis Entry Points for Sucrose Sucrose can enter glycolysis by either of two routes: Sucrose phosphorylase: Sucrose + Pi fructose + glucose-1-phosphate Invertase: Sucrose + H20 fructose + glucose Would either of these reactions offer Jin advantage over the other In the preparation of hexoses fur entry into glycolysis?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%Choose the enzyme and cofactors involved in the reaction of fructose-1,6-bisphosphate to fructose-6-phosphate in gluconeogenesis. H H-TOPO Fo HOTH HDH HOH MOTOPOP K E H-TOH H OPO Problem 3 of 17 A B Q D E fructose-1,6-bisphosphatase phosphoglucose isomerase glucose-6-phosphatase phosphoglycerate kinase hexokinase
- Handwritten Identify the molecule names, enzyme name, enzyme classification and change in reaction(for glycolysis pathway)Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilutionActivity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.
- 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 s1Isoform of Lactate dehydrogenase LDHGTP or ATP is produced during the conversion of isocitrate into ketoglutarate succinyl CoA into succinate fumarate into malate malate into oxaloacetate
- Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.Assessing 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.)