refers to the slowdown of a metabolic pathway when products at the end of such a pathway cross a specific threshold Vmax describes reactions that require free energy to convert reactants into products feedback inhibition the number of substrate molecules that can be converted into products per endergonic second produces Lineweaver-Burke plots that have a common x-intercepts between inhibited and uninihibited enzyme-catalyzed reactions noncompetitive catalysis that includes a proton donor other than water sequential model requires that all substrates bind to the enzyme before any product is released inhibition minimized by increasing substrate concentration competitive enzymes that catalyze reactions joining molecules together ligases enzymes characterized by sigmoidal plots between reaction rate and substrate allosteric concentration switches between binding substrate to the enzyme and releasing product at concentrated model each step

refers to the slowdown of a metabolic pathway when products at the end of such a pathway cross a specific threshold Vmax describes reactions that require free energy to convert reactants into products feedback inhibition the number of substrate molecules that can be converted into products per endergonic second produces Lineweaver-Burke plots that have a common x-intercepts between inhibited and uninihibited enzyme-catalyzed reactions noncompetitive catalysis that includes a proton donor other than water sequential model requires that all substrates bind to the enzyme before any product is released inhibition minimized by increasing substrate concentration competitive enzymes that catalyze reactions joining molecules together ligases enzymes characterized by sigmoidal plots between reaction rate and substrate allosteric concentration switches between binding substrate to the enzyme and releasing product at concentrated model each step

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thx
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?
If you graph the velocity of an enzymecatalyzed reaction vs. [S] for each of two substrates that are partof a random mechanism, would you expect to see the same shapecurve? Why or why not?
Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.
Which of the following statements about enzyme character-istics is true?(a) Enzymes generally exhibit a high degree of specificityfor one particular substrate.(b) Enzyme-substrate complexes occur when a substratemolecule collides with the allosteric site of an enzyme.(c) Chemical bonds within a substrate are strength-ened when this substrate forms an enzyme-substratecomplex.(d) Enzymes have a region called the active site, which pro-vides an area where it can form a loose association withits substrate.(e) a and d.
state a optimum temperature of enzyme E
The reason for the increase in the rate of an enzyme reaction when the temperature is increased isa. decrease in kinetic energy of reactantb. increase in kinetic energy of reactantc. increase in activation energy of reactiond. decrease in activation energy of reaction
A model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?
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.
The Michaelis constant: depends on the concentration of the enzyme. displays the maximal rate of the reaction, when it is much less than the substrate concentration. displays the maximal rate of the reaction, when it is equal to the substrate concentration. displays zero-order kinetics, when the it is equal to the substrate concentration. describes the properties of the enzyme.
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.)
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.