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Interpret clearly and explain the information presented in this graph
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- Determine how reaction rate (velocity) varies with substrate concentration. F3 $ 4 Substrate concentration R F Additional substrate is added when substrate concentration is low. F4 % 5 T Rate increases G 6 HOLL F5 & H 7 F6 YU J *00 8 DELL F7 K ( 9 Substrate is added when enzyme is saturated with substrate. F8 Rate decreases O Answer Bank F9 P W F10 { [ + 11 F11 } 1 F12 Additional substrate is added when substrate concentration is high but is not yet saturating. Backspace Rate is unchanged Enter Insert Print Screen Delete Home Scroll Lock End 8:26 PM 2 10/15/2023 + PgUp Pause Break PgDnAA 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)?please help me understand this practice problem with as much details as possible. An enzyme reversibly binds a substrate. The rate constant (kcat) for catalytic conversion of enzyme- substrate complex into product and free enzyme is 1.0 s-1. The rate constant for dissociation of enzyme- substrate complex (k-1) is 9.0s^-1. 1) For each substrate binding event, what is the probability that substrate is converted into product rather than dissociated without conversion? 2) What is the probability that 20 consecutive binding events result in no product formation? 3) If you evaluated 1,000 different sets of 20 consecutive binding events, what would be the average number of product molecules formed (per 20 binding events)? 4) What is the probability that 20 consecutive binding events result in a number of product molecules at least equal to this average?
- PART IV. HOW FAST DOES IT GO?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. A. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor. B. If GAPDH is inhibited, what specific type of inhibition is observed?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 aprotease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by half
- With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the aboveUSSE EUSS reaction rate substrate concentration Blue line - Enzyme alone Red line - Enzyme + unknown compound The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors. Review the graphs above. Each graph represents the activity of an enzyme and the enzyme + the addition of an unknown compound. By comparing the kinetics of the enzyme alone to the enzyme + unknown, determine what type of compound was added to each of the 4 different solutions to elicit the observed change.Indicate the hinge region, GK kinaseselectivity pocket and explain "Solvent AccessibilitySurface" and indicate the salt forming group at ATPbinding site
- =display&toolld3calendar-mybb, Gmail YouTube Maps calendar-tool Home Courses C A Question Completion Status: 20 3D 70 100| 11凸|12D|| 130 14 150 16 170 QUESTION 14 A newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180KDA and SDS-PAGE shows it to be a homodimer. 1mg of enzyme produces 0.05 mmoles of product per minute per mL. What is the turnover number of this enzyme in µmol product produced per pmol of enzyme subunit per mL? O a. 4.5 Ob.4500 O c. 9000 O d.9 QUESTION 15 The absorption spectrum of NAD" and its reduced form NADH are shown below: Absorption 2,4 2,0 1,6 Click Save and Submit to save and submit. Click Save All Answers to save all answers. Save All Ar 8 11 JAN 9. tv W ... LOLysozyme is a catalytic enzyme that cleaves NAG-NAM units in the bacte- rial cell wall, and is found in external secretions of the body. Why does thisGraph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.