Rearrange the following terms to show the process of enzymatic reaction.Useand + to complete the equation.enzyme enzyme-substrate complexenzymeproductsubstrateSeveral important things should be noted about this reaction:1. A/anbecause of the fit between their structures;2. As a result, something happens to theexample, it might be split in two at a particular location.3. Then theand4. The enzyme isagain.5. Note that the arrows in the formula for enzyme reaction pointacts on a specificto form a/anmolecule. Forcomes apart, yielding thein the reaction and is now free to react_- This means that the reaction is6. An enzyme-substrate complex can simply go back to thethe7. The products of an enzymatic reaction can react with the enzyme toform theandagain;8. It, in turn, may again form the9. Therefore, the same.and themay act to cause ato go eitherway.

An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which…

Answered: Rearrange the following terms to show…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.
Suicide substrates are substances that resemble the substrate,but when incorporated into the active site they form a covalent bond with the enzyme, permanently inhibiting it. Thesemolecules have been used to label the amino-acid side chainsthat are involved in the catalytic reaction occurring withinthe active site. This is usually accomplished by hydrolyzingthe inhibited enzyme. How could an investigator identify theamino acid bound to the suicide substrate molecule?
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?
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.
An enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.
Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.
An uncompetitive inhibitor interacts with the enzyme•substrate complex to form a ternarycomplex (ES•I). This equilibrium reaction can be described as follows:ES + I ⇌ ESIModify the simplified kinetic scheme you drew for E + S ⇌ E + P to include this equilibriumexpression
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
A cat named Lucullus is so spoiled that he willeat nothing but freshly opened canned tuna. Another cat, Griselda, isgiven only dry cat food by her far less indulgent owner. Canned tunais essentially all protein, whereas dry cat food can be considered 70%carbohydrate and 30% protein. Assuming that these animals haveno other sources of food, what can you say about the differences andsimilarities in their catabolic activities?
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.

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