The glycosidic linkage between glucose molecule in maltose is? (in 1 to 3 sentences, explain why this is your answer). A. B1-4 В. а 1—2 С. В1 -2 D. α 1-4
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- 10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.The Hb Yakima variation is caused by the mutation D99H, which results in a shift in oxygen binding as shown in the graph. What effect does the D99H variation have on the [T] / [R] ratio of Hb Yakima protein conformation compared to Hb Normal and how does D99H alter oxygen affinity? Fractional saturation 1.0 2 Hb Yakima 20 Hb Normal 40 60 po, (kPa) 80 100
- The enzyme lysozyme kills certain bacteria by attacking a sugar called N-acetylglucosamine (NAG) in their cell walls. At an enzyme concentration of 2 × 10-6 M, the maximum rate for substrate (NAG) reaction, found at high substrate concentration, is 1 × 10-6 mol L¯'s1. The rate is reduced by a factor of 2 when the substrate concentration is reduced to 6 x 10-6 M. Determine the Michaelis-Menten constants Km and k, for lysozyme.1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…1. A Lineweaver-Burk Plot is shown below. 30 25 Curve A y = 3.1207x + 2.4978 20 15 Curve B y = 1.0003x + 2.3602 10 5 -3 1 5 7 11 1/[Catechol] (mM1) With these curves, determine the following enzyme parameters. Show all pertinent solutions. a. Km of Curve A and Curve B b. Vmax of Curve A and Curve B c. Assuming that one of these curves corresponds to the kinetics of one enzyme and one substrate, which curve represents the effect of an inhibitor? Why do you say so? d. What type of inhibition is exhibited by your answer in question c? Why do you say so? 1/V, (units of activity 1)
- The isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.The compound below, doxorubicin, is a substrate for p-glycoprotein. Cancer cells with a higher expression of P-gp (more P-gp protein per cell) than normal cells were treated with doxorubicin. What would be the expected observation? o= 0= OH O OH HCI OH -OH NH₂ & OH more doxorubicin inside the cell doxorubicin would be oxidized doxorubicin would have more cytotoxic effect on these cancer cells less doxorubicin inside the cell
- The fosfomycin disc (200/50) also contains glucose-6-phosphate (G-6-P). Which ONE of the following best describes why this is the case? Select one: A. G-6-P increases the solubility of fosfomycin B. G-6-P is used to promote active transport of fosfomycin into the bacterial cell C. G-6-P is used in the formulation to correct glucose deficiencies promoted by fosfomycin D. G-6-P stabilises fosfomycin from spontaneous hydrolysis in aqueous solution E. G-6-P is an inhibitor of FosA that inactivates fosfomycinThe enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)A solution of [U 14C] glucose-1-phosphate (specific activity = 16,000 cpm/mmole) was incubated with glycogen and glycogen phosphorylase, an enzyme which adds glucose units on to glycogen. Radioactivity was incorporated into the glycogen primer at a rate = 2550 cpm/min. The rate of the enzymatic reaction in units of mmole glucose incorporated per minute is: (a) 0.016 mmol/min (b) 0.57 mmol/min (c) 0.16 mmol/min (d) 5.7 mmol/min
