Determine how reaction rate (velocity) varies with substrate concentration.F3$4Substrate concentrationRFAdditional substrate is added when substrateconcentration is low.F4%5TRate increasesG6HOLLF5&H7F6YUJ*008DELLF7K(9Substrate is added when enzyme is saturatedwith substrate.F8Rate decreasesOAnswer BankF9PWF10{[+ 11F11}1F12Additional substrate is added when substrateconcentration is high but is not yet saturating.BackspaceRate is unchangedEnterInsertPrintScreenDeleteHomeScrollLockEnd8:26 PM 210/15/2023+PgUpPauseBreakPgDn

Q.Explanation:- Substrate is a specific term for the reactant on which a particular type of enzyme…

Answered: ration Determine how reaction rate…

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 Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The S terms cancel out in this equation, so there is no effect of changing substrate concentration. The S] term in the numerator is negligible, so there is no impact of changing substrate concentration. Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity. OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration and velocity.
please help me understand this practice problem with as much details as possible. An enzyme reversibly binds a substrate. The rate constant (kcat) for catalytic conversion of enzyme- substrate complex into product and free enzyme is 1.0 s-1. The rate constant for dissociation of enzyme- substrate complex (k-1) is 9.0s^-1. 1) For each substrate binding event, what is the probability that substrate is converted into product rather than dissociated without conversion? 2) What is the probability that 20 consecutive binding events result in no product formation? 3) If you evaluated 1,000 different sets of 20 consecutive binding events, what would be the average number of product molecules formed (per 20 binding events)? 4) What is the probability that 20 consecutive binding events result in a number of product molecules at least equal to this average?
The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?
1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
An enzyme with a Km of 3 X 10-4 M was tested at an initial substrate concentration of 10-5 M. In 1 minute, 5% of the substrate was found to be utilized. (a) What percentage of the substrate was utilized in 5 minutes? (b) If the initial substrate concentration had been 8 X 10-7 M, what percentage of the substrate would have been utilized in 5 minutes? (c) Vmax =? (d) How long would it take to utilize 50% of the substrate at 8 X 10-7 M? (e) How long would it take to utilize 75% of the substrate at 10-5 M?
when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
k_1 E + SES E + P +0 k₂ S ↓↑ KIS ESS Based on this model, please answer the following questions: i) This is the model for what? Uncompet tive ii) Show the rate equation for an enzyme reaction of this type. iii) Show the Lineweaver-Burk plot for this case. A
at what substrate concentration is v= 5.0 mM s^-1 for the enzyme catalyzed hydrolysis of trehalose?
-Inhibitor +Inhibitor [S] (mM) V0 &ν βσπ:(μmol/sec) V0&νβσπ: &ν βσπ:(μmol/sec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITHOUT iinhibitor?
-Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITH iinhibitor?

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