Number 4 please 4. What is the enzyme present in the saliva? EFFECT OF ENΖΥΜΕ CONCENTRATIOΝ ON ΕNZΥΜΕ ACTIVITYIntroduction:Enzymes are highly specialized class of proteins. They catalyze thousands ofchemical reactions with remarkable property of speeding up chemical reactions. Theycombine with the reactants to produce a transition state having less energy than thetransition state of uncatalyzed reaction. When reaction products are formed the freecatalyst is regenerated.The rate of enzyme catalyzed reaction is determined by the concentration ofthe enzyme used. The more concentrated the enzyme used, the faster is the reaction.Objectives: At the end of the activity, the student can:1. Determine the effect of different concentration of enzyme on reactionrate2. Compute for the concentration of enzyme present in each tube.3. Determine in which concentration reaction rate is fastest and slowest.Reagents: Saliva, 6 ml 1% starch solution, 6 drops Iz in KI, 6 ml benedict's reagent.Materials: 12 Test tube (20 ml), 10 ml graduated cylinder, test tube rack, brush, 250ml beaker, tripod, wire gauze, thermometer, alcohol lampProcedure:1. Prepare 6 test tubes and place 1 ml saliva in each.2. Add 1ml water to tube 1,2 ml to tube 2, 4 ml to tube 3,6 ml to tube 4, 8 ml totube 5 and 10 ml to tube 6. Mix thoroughly.3. Transfer 1 ml of each into 6 separate test tubes (discard excess solution) andadd 1 ml of 1% starch paste. Mix well and heat in a water bath withtemperature maintained at 40°C for 30 minutes.4. Divide each of the contents of each tube into 2 and test with:a. Iodine Test – to half of the content of each tube, add 1 drop of iodine in KIand note the color produced. Compare the intensity of color in each of the6 tubes.b. Benedict's – to 1 ml benedict's reagent, add 5 drops of the other half ofeach tube and heat in a boiling water bath for 3 minutes. Note color ofprecipitate.5. Rank each tube according to decreasing reaction rate one (1) being the fastestto hydrolyze and 6 being the slowest.

Enzymes are the biocatalysts that speed up biochemical reactions at optimum pH and temperature.…

Answered: What is the enzyme present in the…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter21: Photosynthesis

Section: Chapter Questions

Problem 15P

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multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation:1. kcat >> k1 or k-12. In the presence of a negative allosteric effector3. At low concentrations, the reaction is first order with respect to substrate concentration4. At high concentrations the reaction is zero order with respect to substrate
In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.
the enzyme dUTPase from the African swine fever virus (ASFV), which is a virus that spreads rapidly in swine (pigs) and is often deadly. The normal function of the dUTPase enzyme is to convert dUTP to dUMP. Which of the following statements about the dUTP substrate for a dUTPase is true? Explain your choice in 25 words or less. The dUTP substrate binds with lower affinity to the enzyme than the dUMP product The dUMP product is more easily formed when catalyzed by the dUTPase because the equilibrium is shifted away from the dUTP substrate The formation of the dUTP-dUTPase complex is driven by entropy More than one of the above statements is true None of the above statements is true
Modified 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).
BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Supposed you want to use phosphoglucomutase to breakdown glycogen. You found out that this enzyme is responsible for converting glucose 1-phosphate (C6H13O9P) to glucose-6-phosphate (C6H13O9P). Based on this action, to which enzyme class does phosphoglucomutase belong? A. Isomerase B. Oxidoreductase C. Lyase D. Ligase
A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?
Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!
Kinetics of enzymatic reactions: the dependence of the reactionrate on the concentration of enzyme and substrate, рН andtemperature. Kinetics of allosteric enzymes
BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the transition state of a catalyzed reaction? A. higher in energy than that of an uncatalyzed reaction B. lower in energy than that of an uncatalyzed reaction C. bound very weakly to the catalyst D. lower energy than the reaction substrate
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase
Serine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surely

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