48 The six groups of enzymes are the following: I. Oxidoreductases II. Transferases II. Hydrolases IV. Isomerases V. Lyases VI. Ligases Fill in the blanks: catalyze transfers of groups while catalyze bond breakages. (2 Points) O Il and V O Il and VI O V and II O IV and II O Il and IV 49 Common Saturated Fatty Acids: Lauric acid: CH3(CH2)10CO2H Myristic acid: CH3(CH2)12CO2H Palmitic acid: CH3(CH2)14CO2H Stearic acid: CH3(CH2)16CO2H Arachidic acid: CH3(CH2)18CO2H Refer to the condensed formula for saturated fatty acids to be able to generate the name of the triglyceride below * (3 Points) CH2OCH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH3 CHOCH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH3 ČH2OČCH,CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH,CH2CH2CH3 O glyceryl trilaurate O glyceryl trimyristate O glyceryl tripalmitate O glyceryl tristearate ООО O O O O

48 The six groups of enzymes are the following: I. Oxidoreductases II. Transferases II. Hydrolases IV. Isomerases V. Lyases VI. Ligases Fill in the blanks: catalyze transfers of groups while catalyze bond breakages. (2 Points) O Il and V O Il and VI O V and II O IV and II O Il and IV 49 Common Saturated Fatty Acids: Lauric acid: CH3(CH2)10CO2H Myristic acid: CH3(CH2)12CO2H Palmitic acid: CH3(CH2)14CO2H Stearic acid: CH3(CH2)16CO2H Arachidic acid: CH3(CH2)18CO2H Refer to the condensed formula for saturated fatty acids to be able to generate the name of the triglyceride below * (3 Points) CH2OCH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH3 CHOCH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH3 ČH2OČCH,CH2CH2CH2CH2CH2CH2CH2CH2CH2CH2CH,CH2CH2CH3 O glyceryl trilaurate O glyceryl trimyristate O glyceryl tripalmitate O glyceryl tristearate ООО O O O O

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.75E: In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent...

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How can distance validate non-covalent interactions? Also, please explain if the distance between c-alpha of a particular residue in an enzyme and c-alpha of its ligand are 12.4 Å, 11.7 Å, 6.5 Å, 7.6 Å, and 7.7 Å, what does that mean? What is the meaningful distance, what is the legth of hydrophobic,hydrophilic, h-bond...?
For the reaction 2Na (g) Na2 (g) the following values of K have been determined (C. T. Ewinget al., J. Chem. Phys. 1967, 71, 473):T (K) K900 1.321000 0.471100 0.211200 0.10From these data, estimate rxnH° for the reaction.
4 1. Use the Michaelis-Menten equation to explain relationship between the amount of product produced and the concentration of enzyme in each reaction. 2. Briefly explain how you would modify the experiment performed in part C to determine the Km and Vmax of the lactase enzyme ANSWER BOTH
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)
We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer
4-1Based on the experimental results shown in the table, Identify whether the inhibitor acting on this enzyme is acompetitive inhibitor or a non-competitive inhibitor, and Explain the reason logically. 4-2In 4-1, the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
Aleks data for PbCO3 is 7.40 x 10^-14.
15.1 mg of β-carotene resulted in a blood plasma level of 43 nmol L-1 of Vitamin A.100% of the β-carotene is converted to Vitamin A (286 g mol-1), and that absorption of β-carotene occurs predominately in the small intestine in an aqueous volume of 600 mL, estimate the equilibrium constant for the reaction below:the ratio is 2 molecules of Vitamin A converted by enzymes from 1 molecule of β-caroteneVitamin A (intestine) ⇌Vitamin A (plasma)
Many enzymes are inhibited irreversibly by heavy metal ions such as Hg2+, Cu2+, or Ag+, which can react with essential sulfhydryl groups to form mercaptides: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 1.0 mg/mL of a pure enzyme, an investigator added just enough AgNO3 to completely inactivate the enzyme. A total of 0.342 μmol of AgNO3 was required. Calculate the minimum molecular weight of the enzyme. Why does the value obtained in this way give only the minimum molecular weight?
Calculate the specificity constant for an enzyme-catalyzed reaction if the total enzyme concentration is 15 nM, Vmax is 9 M/s, and Km is 150 M. A. Has the enzyme achieved catalytic perfection? (Y or N)
calculate the Keq of a reaction that has a DeltaG of 8.8 kJ/mol at 25C.
Calculate the value of the denaturation constant kd for a given enzyme, using the equation provided from the text and lecture of kd = Ad e(-Ed/RT) where Ad = 6.1 x 1047 and Ed = 69 kcal/g mole. Then, prepare a plot of per cent enzyme maximal activity vs temperature using an Ea of 23 kcal/gmole, and an enzyme concentration E0 of unity. Note that the y-axis of this plot is a per cent value, so the value of A in the Arrhenius equation does not need to be known in this case. On the denaturation side of the curve, use 5 minutes as the constant exposure time. Use a temperature range of 20 to 50⁰C.