Which of the following are true when enzymesand substrate interact?kıE + S●ES--Pk-1the rate of the formation of ES = k1 [ES]the rate of the formation of the product = k2[ES]k1 [ES] = k-1 [ES]the rate of breakdown of ES to reform theenzyme and substrate = K-1[E][S]the rate of formation of ES = k1[E][S]

Assuming the enzyme follows the first order kinetics, The rate of a formation is given by the…

Answered: Which of the following are true when…

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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Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
For the following problem, indicate whether enzyme is repressed (-) or produced (+). Please show all possible outcomes.
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
What statement about states of the allosteric enzyme is TRUE? The value of KM for the T state is lower than for the R state. O The value of Vmax for the T state is lower than for the R state. O The value of KM for the T state and the R state is the same. The value of Vmax for the T state is higher than for the R state. O The value of KM for the T state is higher than for the R state.
In a bisubstrate reaction, a small amount of the fi rst product P is isotopically labeled (P*) and added to the enzyme and the fi rst substrate A. No B or Q is present. Will A (= P—X) become isotopically labeled (A*) if the reaction follows a Sequential mechanism?
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
The 2 eynzymes are affected by a substrate. Choose all correct answers.
J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala
Discuss in a short paragraph (3–5 sentences for each mutation) whether or not the enzyme is likely to completely lose catalytic activity if the following mutations are carried out. You may assume that steric effects do not distort the active site so much that catalysis cannot take place; focus your analysis on discussing the chemistry the amino acid side chains are able to perform and the properties that enable them to do so. Mutation 1: H to E Mutation 2: H to N Mutation 3: S to D Mutation 4: S to C
The pathway shown below is used by a fungus to create Fructose-1,6-diphosphate from glucose. A silent mutation occurs in the gene that encodes enzyme 3. This fungus is grown on media that only contains the precursor. Discuss the effects of this mutation on: (i) The function of Enzyme 3 (ií) The production of Fructose-1,6-diphosphate Enzyme 1 Glucose-6- Enzyme 2 fructose-6- Enzyme 3 Fructose-1,6- Glucose phosphate phosphate diphosphate

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