The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by adeacylation reaction.What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenylester by chymotrypsin?The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate.The rates of the acylation and deacylation reactions are equal.The rate of the acylation reaction is slower than the rate of the deacylation reaction.The rate of the acylation reaction is faster than the rate of the deacylation reaction.

A burst in rapid kinetic studies (i.e. pre-steady state studies) is a high rate of product release…

Answered: The mechanism of chymotrypsin can be…

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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Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
Determine whether the following reactions will be spontaneous under standard biochemical conditions. Include calculations for Delta G in your answer. Use Table 13-7 in your textbook to help you.a) 2NADH + 2H+ + O2 --> 2NAD+ + 2H2Ob) Malate + FAD --> Oxaloacetate + FADH2c) Pyruvate + H2S --> Lactate + S
What is the quaternary structure of glycogen phosphorylase? How would you characterize the allosteric effects of its small molecule substrate? (one word) What allosteric model (mechanism) that you have learned does it seem to follow? (one acronym)
Considering that triacylglycerols get hydrolyzed in the small intestine because of pancreatic lipases, write the reactions using structural formulas by which a 7-carbon fatty acid is activated and oxidized in the liver of this patient. Indicate cofactors and underscore the final CoA products.
The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
Why is triose phosphate isomerase considered to be catalytically perfect?
Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase.
This is a picture of the catalysis of alcohol by ADH with an inhibitor binding as an aldehyde analog. I have two questions. First, what would the enzyme be classified as and why? Also, what would the steps of this mechanism be?
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
Suppose a liver extract capable of carrying out normal metabolic reactions (including gluconeogenesis) is incubated with pyruvate partially labeled with deuterium at the methyl group (see below: D= deuterium, i.e., H-2) a) Explain why the oxaloacetate formed in step 1 of gluconeogenesis is only partially labeled (i.e., some of the oxaloacetate is labeled and some is not). b) Where would the label be found in glucose?
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…

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