A certain enzyme has two binding sites A and B, and two conformational states. That is, it can take on two different shapes:State1State2ВThe substrate of the enzyme looks like this:Which site is the active site?Click the tabs to see each state.AB(neither A nor B)Classify each of the following molecules.(Check all categories that each molecule could be in.)O substratecompetitive inhibitornoncompetitive inhibitorsubstratecompetitive inhibitornoncompetitive inhibitorX A certain enzyme has two binding sites A and B, and two conformational states. That is, it can take on two different shapes:State1State2The substrate of the enzyme looks like this:Click the tabs to see each state.

Enzymes are catalyst in the biological system that participate in biochemical process and they are…

Answered: A certain enzyme has two binding sites…

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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The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate facilitate the catalysis of chemical reactions. Which of the following properties of enzyme-substrate interaction best explains enzymatic catalysis according to the induced-fit model? A B с D Environmental conditions can alter the affinity between a substrate and an enzyme by changing the conformation of the enzyme. Conformation changes in both the enzyme and the substrate due to their chemical in- teractions lower the activation energy of the catalyzed reactions. The interactions between an enzyme and a substrate depend on both structural and chemical compatibility and are therefore highly specific. Enzymes remain chemically unaltered between cycles of enzymatic catalysis while sub- strates are transformed into products.
A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?
on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer a competitive inhibitor the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) a noncompetitive inhibitor an allosteric effector The effect of O 2 3 $ 4 G Search or type URL 67 dº % 5 MacBook Pro 6 7 * CO 8 -o .. E
Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weight
The effect of on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) an allosteric effector a noncompetitive inhibitor a competitive inhibitor
Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
A) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)
None
This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?
Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins
Researchers have identified an enzyme that can catalyze two different chemical reactions. Which of the following is most likely true based on this finding? A B C D The reactants involved in the two reactions are very similar in their charge and shape. The reactant in one reaction acts as an allosteric inhibitor while the reactant in the sec- ond acts as an allosteric activator. The enzyme contains both alpha-helices and beta-sheets in their secondary structures. The catalytic activity of the enzyme is dependent on both competitive inhibition and al- losteric regulation.
Graph a double reciprocal plot that satisfy the following: a. Michaelis-Menten kinetics enzyme, b. an inhibitor that binds only free enzyme (competitive), c. an inhibitor that binds only enzyme-substrate complex.

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