(a)
Interpretation:
The effect in the rate of an enzyme-catalysed reaction has to be determined if temperature is decreased from
Concept Introduction:
Enzyme:
- It is a protein or a molecule which can act as a catalyst for a biological reaction.
- Does not affect the equilibrium point of the reaction.
- Active site of the enzyme is the region where the reaction takes place.
- Enzyme’s activity can be specific which means the activity is limited to a certain substrate and a certain type of reaction and it is referred to as specificity of the enzyme.
Factors affecting enzyme activity:
Substrate concentration
Enzyme concentration
Temperature
(b)
Interpretation:
The effect in the rate of an enzyme-catalysed reaction has to be determined if a drop of dilute
Concept Introduction:
The competition of an enzyme can be reversible or irreversible and in reversible inhibition, the inhibitor can leave and in irreversible inhibition, the inhibitor remains permanently bound.
Reversible Competitive inhibition: It is a type of inhibition occurs when the inhibitor resembles very much to the substrate and thus prevents the substrate binding.
Irreversible competitive inhibition: It is a type of inhibition in which an inhibitor forms covalent bonds to the active site and thereby permanently blocking it.
(c)
Interpretation:
The effect in the rate of an enzyme-catalysed reaction has to be determined if oxidising agent such as
Concept Introduction:
Enzyme:
- It is a protein or a molecule which can act as a catalyst for a biological reaction.
- Does not affect the equilibrium point of the reaction.
- Active site of the enzyme is the region where the reaction takes place.
- Enzyme’s activity can be specific which means the activity is limited to a certain substrate and a certain type of reaction and it is referred to as specificity of the enzyme.
Factors affecting enzyme activity:
Substrate concentration
Enzyme concentration
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FUNDAMENTALS OF GENERAL CHEM VOL 2
- In a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?arrow_forwardWhat general effects would you expect the following changes to have on the rate of an enzyme-catalyzed reaction for an enzyme that has its maximum activity at body temperature (about 37 °C/310.15 K)?(a) Raising the temperature from 310 K (37 °C) to 343 K (70 °C)(b) Lowering the pH from 7 to 3(c) Adding an organic solvent, such as methanolarrow_forwardAre enzyme-catalyzed reactions examples of homogeneous or heterogeneous catalysis?arrow_forward
- At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?arrow_forwardAn uncatalyzed reaction progresses at a rate of 20micromoles per minute while the same reaction in the presence of an enzyme progresses at a rate of 100micromoles per second. What is the rate enhancement achieved by the presence of the enzyme? At 25oC, how much energy is required to produce a 10-fold rate enhancement? At the same temperature, how much energy is required to produce a million-fold rate acceleration?arrow_forwardWhat are the rate constants for the enzyme-catalyzed reaction?arrow_forward
- You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.arrow_forwardThe following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?arrow_forwardConsider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.arrow_forward
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