Please answer all parts in detail. Give explainations. Thanks. The enzyme aspartate transcarbamoylase (ATCase) catalyzes the reaction below and, as discussed in class and in the text, is a prototypicallosteric enzyme.+NH3Asp+на доровH₂NCPATCaselupΝΗH₂N+20HPO4a. Classify this enzyme into one of the 4 categories of biochemical reactions.b. Sketch, on a single plot, separate curves of the velocity vs. [aspartate] for the native enzyme and enzyme that has been treated with amercurial. You should assume that [carbamoyl phosphate] is the same for each curve, and is < Ko.5. Briefly explain why these plots aredifferent.c. Sketch, on a single plot, separate curves of the velocity vs. [aspartate] for the enzyme in the absence of effectors and in the presence ofCTP and ATP. You should assume that [carbamoyl phosphate] is the same for each curve, and is < Ko.5.d. Sketch, on a single plot, separate curves of velocity vs [CTP] and velocity vs [ATP]. In both cases assume low concentrations (e. < K0.5) ofboth aspartate and carbamoyl phosphate.

The 4 main categories of biochemical reactions are;Neutralization : reactions between an acid and…

Answered: The enzyme aspartate transcarbamoylase…

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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Gout is a medical condition usually caused by a deficiency of the salvage enzyme hypoxanthine-guanine phosphoribosyltransferase. Uric acid accumulates in the joints and causes pain, inflammation, and in advanced disease gouty tophi. Allopurinol, an inhibitor of the enzyme xanthine oxidase, is used to treat chronic gout. Explain briefly the biochemical basis for this treatment.
Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.
Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.
The enzyme ATCase (Aspartate TransCarbamoylase) catalyzes an early step in the synthesis of the pyrimidine nucleotides. The activities of the ATCase reactions are shown in the following plots. Which one of the following statements is most correct description about this enzyme and/or this enzyme-catalyzed reaction? ATP No allosteric effectors Vo CTP ATCase 10 20 30 40 (Aspartate] (mM) O A. This enzyme is allosterically inhibited by ATP. B. This enzyme is composed of multiple subunits. C. "ATP" binds to catalytic subunits of ATCase. O D."CTP" binds to the R-state enzyme. O E. At high concentrations of ATP, ATP binds to the T-state enzyme, thus increase the affinity for the substrate [S].
Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess uses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student searcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO hich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the neweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table Table 1. Enzyme Kinetic Data Velocity, mM/s Kmp 0.0351 [S], mM Cha Хan 0.492 0.0678 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Enzyme Kinetic Parameter: Parameters Vmax |Ku | Type of Inhibition Mode of Binding Xanthine Kaempferol Chlorogenic acid NA NA Line Weaver Burk Plot:
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…
The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a phosphorylatedenzyme intermediate. If 3-phosphoglycerate is radioactively labeledwith 32P, the product of the reaction, 2-phosphoglycerate, does nothave any radioactive label. Design a mechanism to explain these facts.
Mechanisms of catalysis : 2.1 Acid-base catalysis summary + example 2.2 Electrostatic catalysis summary + example 2.3 Covalent catalysis summary + example 2.4 Enzymen catalysis summary 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) 2.6 Mechanism of lysozyme 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.…
There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
The catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.

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