(a)
Interpretation:
A double-reciprocal plot which corresponds to the velocity-versus-substrate curveneeds to be plotted.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
(b)
Interpretation:
A plausible explanation that corresponds to the kinetic results shown by Michaelis-Menten enzyme needs to be stated.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
Want to see the full answer?
Check out a sample textbook solutionChapter 8 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
- Required partner. Aminotransferases require which of the following cofactors: a. NAD+/NADP+NAD+/NADP+ b. Pyridoxal phosphate c. Thiamine pyrophosphate d. Biopterinarrow_forwardFill in the blanks.: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.arrow_forwardOH affromah. The Standard free energy CAGO¹) of the reaction shown above can be estimated based on? OH A. High Energy bands B. Reduction potential C. cannot be estimated OH energy. он The reaction shown above requires the cofactor to proceed forward without significant was te of A.ATP B. Nicotinamide C. Flavin D. No cofactor required 3 Determine approximate 46°1 of the coupled reaction KJ/mol possible answers: (0,-8,-15,-22,-30, -38,-45) The class of enzyme that catalyzes the reaction is possible answers: Mutase, Isomerase, ki nase, phosphatase, Dehydrogenase, Aidolasearrow_forward
- In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forward6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forwardFor 100 words. What are the two essential requirements to effectively carry out metabolic work?arrow_forward
- A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)arrow_forwardA7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.arrow_forwardModified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).arrow_forward
- Help please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forwardEach plot has its own limitations. Match the plot with the correct statement on limitations. 1.Hanes-Woolf 2.Michaelis Menten 3.Lineweaver-Burk limitations: A. This plot appears to allow for more accurate calculation of these parameters, but is prone to error, as the y-axis takes the reciprocal of the rate of reaction –this increases any small errors in measurement at low substrate concentration, where they are most likely to occur. B.The advantage of this plot is that it does not not overemphasizing the data obtained at low [S]. The disadvantage is that any inaccurate measures of substrate concentration will be exaggerated as [S] is used on both axes. C.It is difficult to obtain a meaningful value of Km from this plot because of the high substrate concentrations needed to reach Vmax. Vmax has to be estimated by extrapolation- which is partly subjective and introduces error. D.The advantage of this plot is that it overcomes uneven spacing of points, and undue weight of a…arrow_forwardX Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON