Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 10, Problem 33P
Interpretation Introduction
Interpretation:
The significance of the alteration in the given absorbance of nitrotyrosine after the addition of the substrate analog succinate at
Concept introduction:
The concerted model suggests that subunits of enzymes are arranged in such connection in which any conformational change in any of the subunit is compulsorily granted to all the subunits.
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please very soon full explanation all parts please
1a. Add to this drawing the substrate molecule binding to the active site and be specific about the shape of the substrate molecule. Next to your drawing write the chemical properties of the substrate that are important for it to bind to the enzyme.
1b. If the amino acid serine present in the active site were to be mutated to valine, how will this mutation affect the enzyme’s activity? Explain in 30 words or less.
1c. Your colleague would like to design an inhibitor molecule for the normal version of this enzyme that targets the enzyme active site.
What are two characteristics of the inhibitor that you would suggest they incorporate in order to allow it to maximally block the enzyme’s activity? Use 40 words or less.
8.Choose the False statement about enzyme binding sites
Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site.
In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other.
In principle, allosteric ligands can have structures that do not resemble those of substrates.
Ligand binding at an allosteric site can cause a conformational change of an enzyme.
Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.
NO AI GENERATED RESPONSE I NEED EXPERTS!!
using results for experiment below conduct 1 graph of the different factors vs rate of enzyme activity. *
*NO FUNNEL GRAPHS ACTUAL GRAPH WITH GOOD TITLE , AND MAKE SURE IT LOOKS LIKE THE IMAGE I PLACED BELOW**
important info:
experiment procedure:
The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0.
To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of…
Chapter 10 Solutions
Biochemistry
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
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- 9:34 AM You sent Help me with this one Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…arrow_forwardChoose False during an enzyme catalyzed reaction. Substrate concentration is typically much larger than that of enzymes. The rate of enzymatic reaction is related to the concentration of ES complex. Velocity of reaction reaches a plateau above certain substrate concentration. Velocity of reaction is linearly dependent on a substrate concentration. Maximum velocity is related to the number of catalytic turnovers in the unit time.arrow_forwardMultiple choice correct answer and explain every point 2. The factors that contribute to the enhancement of the rate of reactionsa) Specific inhibitor macromoleculesb) Product inhibitionc) Availability of substrate and activator cofactord) Covalent catalysise) Proximity and orientation effectsarrow_forward
- 8 of 15 An enzvme has an all-important histidine residue in its active site such that substitution with an other amino acid would result to the loss of catalytic activity. What are the possible mechanisms by which this histidine residue may facilitate catalysis? I. Acting as proton acceptor. II. Forming of covalent bond with the substrate via an ester bond. III. Serve as stabilizer of electrophilic substrate because of its nucleophilic character. Select the correct response: land II Il and III land IlI I. Il, and IIIarrow_forwardExplain Why and How Questions???Give the reasons and examples!!Add Structures too!1- Enzymes behavior changes during Michalis Mentin curve?2- Lyase is typically opposite ligase enzymesarrow_forward1C One of the major findings of this study is that GTP arrests the enzyme. Draw (i) the natural substrate ATP; (ii) the substrate analog, GTP, and (iii) the GMP-PCP molecule. Indicate where they are different. For each molecule, indicate where the hydrolysable (scissile bond) is located. Please help mearrow_forward
- I need help with parts d-g a.) For Ado: catalytic efficiency = 4.18 x 106 M-1s-1 For ATP: catalytic efficiency = 12.1 x 107 M-1s-1 b.) Both specificity constants are below the diffusion limit so neither substrate is limiting the reaction rate due to diffusion c.) Line weaver Burk equation for AdoK enzyme with Ado substrate: y = 0.68x + (2.04 x 104), where y = 1/vo and x = 1/[Ado]arrow_forwardModified 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 reaction involving the substrate bound to the active site of an enzyme is made more favorable by increasing the activation energy of the reaction.arrow_forwardChymotrypsin information about enzyme? Trivial/Common Name Systematic (EC) name and number Chemical reaction catalyzed Metabolic pathway Function and cellular localization Size (kDa) and structure (tertiary and quaternary) pH stability Kinetic properties (Km- and Kcat value/s for natural substrates) Stability and potential inhibitorsarrow_forward
- Enzyme Kinetics question Enzyme used is 10uL of a 10 ng/uL solution to a reaction mix in a final volume of 2.0 mL. (Enzyme used is 20kDa monomeric enzyme if matters) Based off lineweaver burk where 300 uM of inhibitor is used noninhibited formula is y= 4x + 0.1 (x axis is 1/S 1/mM) (y axis is 1/Vo sec/mM) inhibited formula is y = 4x + 1 I found Km as 1 mM for inhibited Vmax as 1mM/sec for inhibited How would I find Kcat? How would I find Ki?arrow_forwardMechanisms of catalysis: 2.5 Mechanism of chymotrypsin summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state)arrow_forwardI have glucoseoxidase 1000 Udl-1. What is the exact unit of the enzyme that could work for 1 micromole of substrate.arrow_forward
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