(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
Want to see the full answer?
Check out a sample textbook solutionChapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- For the following two scenarios, sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction. For each of these, overlay the free energy diagram for the uncatalyzed reaction and indicate AAG" on your sketch: a). Substrate binding is rate limiting b). The chemical step is rate limitingarrow_forward(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.arrow_forwardGiven the following enzyme-catalyzed reaction, identify the class and subclass of the enzyme involved. HO Class: [Select] COO™ NH3* Subclass: [Select] H₂O H₂C= COO™ NH3*arrow_forward
- Consider the enzyme pancreatic amylase, which has an optimum pH of 7.0. How is the rate of a pancreatic amylase-catalyzed reaction affected by each of the following changes: (a) lowering the pH from 7 to 4; (b) increasing the pH from 7 to 9; (c) decreasing the temperature from 37 °C to 28 °C; (d) increasing the temperature from 37 °C to 50 °C?arrow_forwardYou have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!arrow_forwardThe value of Vmax for an enzyme-catalyzed reaction: A) most often reflects the chemical steps of catalysis B) can be determined from initial velocities that are linear with respect to substrate concentration OC) is limited only by the amount of substrate supplied D) can be converted to kcat/Km by accounting for the enzyme concentration OE) is higher for enzymes that also exhibit higher Km valuesarrow_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_forwardWhen enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.arrow_forwardWhich of the following is TRUE under the following conditions: the enzyme concentration is 2.5 nM, substrate concentration is 75 nM, the KM = 150 nM, and the Vmax = 20 nmol/min a) The rate of the reaction is 20 nmol/min! b) The rate of the reaction is between 10 nmol/min and 20 nmol/min. c) The rate of the reaction is 10 nmol/min. d) The rate of the reaction is below 10 nmol/min. e) The rate cannot be determined from the above information.arrow_forward
- An enzyme with an unknown reaction mechanism has been isolated and is being investigated in the lab. Based on the information given below, propose one or more specific catalytic strategies (covalent, acid-base, and/or metal ion catalysis) used by the enzyme and predict the role of each catalytic residue in the enzyme's reaction cycle. Explain your reasoning. (a) Mapping of the active site with substrate analog showed that it contains a critical Ser residue. (b) Studies conducted in buffers of varying pH showed that the enzyme is sensitive to pH changes and has two catalytically important residues with pKa values of ~10.5 and ~4.0. (c) Substitution of the Ser residue with Ala resulted in a five-fold increase in the KM but had no effect on the kcat. (d) The reaction rate was insensitive to the addition of metal chelators such as EDTA and EGTA.arrow_forwardAfter purifying alkaline phosphatase, you perform enzyme kinetic experiments with and without an inhibitor to obtain the following plot: With inhibitor Without inhibitor 1/V (1/mM min?) 0.3 0.2 -150 -100 -50 50 100 150 200 250 300 1/s (1/mM) a) What is the name given to this type of enzymatic plot? b) Using the graph, calculate K_ and V_ inhibitor. Show all calculations. for the enzyme, with and without the maxarrow_forwardSelect the following enzymes that utlize a mechanism involving covalent catalysis. Select ALL that apply: a) aldolase class 1 b) glyceraldehyde 3 phosphate dehydrogenase c) aldolase class 2 d) triose phosphate isomerase e) hexokinasearrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON