Q1: the following table gives the results of enzyme-catalyzed reaction.The enzyme concentration [E] = 0.00012 mmol/LUse the information of substrate concentration [S] and rate Vo for both experiments, withinhibitor and without inhibitor to answer the following questions(NOTE: [E] =0.00012 mmol/L)[S], mmol/L0.7100.4000.3100.0980.0660.040Experiment 11without inhibitorVO, mmol/L-min0.2000.1800.1600.1200.1000.070Experiment 2with inhibitor[1] = 0.033 mmol/LVO, mmol/L-min0.1800.1500.1100.0700.0500.0401- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs Vo2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/vo3- Calculate Kcat for the enzyme (without inhibition)4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine thetype of the Inhibition (competitive, non-competitive or uncompetitive)

The objective of this question is to calculate the Vmax and Km of the different reaction kinetics.…

1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs Vo 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/vo 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive)

1- Calculate Km and Vmax for both experiments using Michaelis-Menten equation. [S] vs Vo 2- Calculate Km and Vmax for both experiments using Lineweaver-Burk plot, 1/[S] vs 1/vo 3- Calculate Kcat for the enzyme (without inhibition) 4- Based on the values of Km and Vmax, with inhibitor and without inhibitor, determine the type of the Inhibition (competitive, non-competitive or uncompetitive)

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

What is the relative activite and the degree of inhibition caused by a competitive inhibitor when [S] = Km and [I]=ki?
Please answer C and D.
Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intracellular abundance. Describe a quantitative approach to determine the number of molecules of an enzyme per cell.
An enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5
Enz-SH + Ag* - Enz-S-Ag + H* The affinity of Ag* for sulfhydryl groups is so great that Ag* can be used to titrate -SH groups quantitatively. To 10.0 mL of a solution containing 3.5 mg/mL of a pure enzyme, an investigator added just enough AGNO, to completely inactivate the enzyme. A total of 0.536 umol AGNO, was required. Calculate the minimum molecular weight (M,) of the enzyme. minimum M, = The determined M, is not exact, but it is a minimum value for the M, of the enzyme. Why does the M, value obtained this way give only the minimum molecular weight? There is only one polypeptide chain. There are no disulfide bonds in the protein. There is only one titratable -SH group per protein molecule. The Ag* would also react with the terminal carboxyl group.
help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working
Shown below is the amino acid tyrosine in its protonated state, with the pK of each ionizable proton indicated. pK = 10 HO H₂N pK = 9 COOH pK = 2 Which best represents the predominant state of tyrosine at pH 7? a HO b B C HO d HO Time left 0:20:16 H.N COOH HN COO HN COO HN COO
Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% alanine (Mr 89.1). Calculate how many alanine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number.
Could someone explain what this is saying? I would like a better understanding. FIGURE D CPP32 (Caspase-3) protease activity. Aliquots of cell lysates (50μL) were incubated with an equal volume (50 μL) of the reactionbuffer and 5 μL of 7-amino-4-trifluoromethyl coumarin (AFCDEVD) for 1 hour at 37˚C (Clontech). The shift in fluorescenceemission of AFC-DEVD, on its proteolysis to free AFC by theprotease, was detected in a fluorometer, using a 400 nm excitationfilter and 505 nm emission filter.
The Km value of an enzyme is affected in the presence of a competitive inhibitor because it requires less substrate to achieve the same Vmax as without the inhibitor. True False
The isoelectric point, pl, of the protein soybean trypsin inhibitor is 4.5 , while that of clostripain is 4.8 . What is the net charge of soybean trypsin inhibitor at pH 5.1 ?[ What is the net charge of clostripain at pH 2.5 ?[ The isoelectric point of tyrosine is 5.66 ; tryptophan , 5.89. During paper electrophoresis at pH 4.5 , toward which electrode does tyrosine migrate? [ During paper electrophoresis at pH 6.5 , toward which electrode does tryptophan migrate?
sub= 18 help