The following diagram shows reaction curves for aspartate transcarbamoylase(ATCase) with carbamoylphosphate and different concentrations of aspartate, in theabsence of ATP (curve 1) and presence of ATP (curve 2). What do the shapes of thecurves tell us about the ATCase enzyme?2جر[aspartate]It binds substrate through a sequential mechanism.It binds substte cooperatively.It obeys Michaelis-Menten kinetics.It binds substrate through a concerted mechanism.

Allosteric enzyme is the class of regulatory enzyme which increases or decreases catalytic activity…

Answered: The following diagram shows reaction…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
When ATP and xylose are added to hexokinase, the enzyme produces a small amount of xylose-5-phosphate along with a large amount of ADP. How does this observation support the induced fit model?
Because it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?
The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?
Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*
Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (Vo) for all six of these experiments: [I] [S] Vo 1/[S] 1/ Vo 0 mM 0.1 mM 0.333333333333 mM per minute 0 mM 0.2 mM 0.50 0 mM 0.3 mM 0.60 0 mM 0.4 mM 0.666666666667 0 mM 0.5 mM 0.714285714286 0.1 mM 0.1 mM 0.20 0.1 mM 0.2 mM 0.333333333333 0.1 mM 0.3 mM 0.428571428571 0.1 mM 0.4 mM 0.50 0.1 mM 0.5 mM 0.555555555556 0.20 mM 0.1 mM 0.142857142857…
The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*
Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor B for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor B (plus the control, with zero mM of inhibitor B). The following Table lists the inhibitor B concentrations [I], substrate concentrations [S], and resulting enzyme velocities (Vo) for all six of these experiments: [I] [S] Vo 1/[S] 1/ Vo 0 mM 0.1 mM 0.333333333333 mM per minute 0 mM 0.2 mM 0.50 0 mM 0.3 mM 0.60 0 mM 0.4 mM 0.666666666667 0 mM 0.5 mM 0.714285714286 0.1 mM 0.1 mM 0.25 0.1 mM 0.2 mM 0.333333333333 0.1 mM 0.3 mM 0.375 0.1 mM 0.4 mM 0.40 0.1 mM 0.5 mM 0.416666666667 0.20 mM 0.1 mM 0.20 0.20 mM…
The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. CH, OH OH - DMB 2e (8 Coa+ он он A -DMB DMB CH, Åderine АТР P + PP, -DMB (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme Cwould result in excessive urinary excretion of what compound? (c) Some forms of the condition described in (b) can be successfully treated by injection of rather massive doses of vitamin B12. What kind of genetic alteration in the enzyme would be consistent with this result? (d) Genetic deficiency in animals of ezyme B will result in excessive uri- nary excretion ofwhat amino acid?
In the hydrolysis of ATP to ADP and Pi, the equilibrium concentration of ATP is too small to be measured accurately. A better way of determining K’eq, and hence ΔG◦’ of this reaction, is to break it up into two steps whose values of ΔG◦’ can be accurately determined. This has been done using the following pair of reactions (the first being catalyzed by glutamine synthetase): (1) ATP + glutamate + NH3 ⇌ ADP + Pi + glutamine + H+ ΔG1◦’= -16.3 kJ/mol (2) glutamate + NH3 ⇌ glutamine + H2O + H+ ΔG2◦’= 14.2 kJ/mol What is the ΔG◦’ of ATP hydrolysis according to these data and is the overall reaction spontaneous? What is the value of the equilibrium constant for the overall reaction at 25.0 °C. If the concentration of ATP at equilibrium is 20.0 mM and the concentration of ADP at equilibrium is 50 nM. What is the concentration the phosphate group (in mM) at equilibrium?

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