3 Consider the reaction shown below and answer the questions that follow.
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Solved in 3 steps
- 1. Answer the following questions, based on this reaction: S +E ES EP E +P A)What is the slow step of this reaction, and why is that step slow?Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…Given the following reaction, identify the class of the enzyme involved. CH,O-PO, CH,OH 2- OH OH OH OH OH Ó-PO,2- OH OH class: [Select] EPIC Ps Ai
- 6. Consider the reaction: H H SCOA a. What kind of reaction is being performed here? b. What enzyme performs this reaction? c. What cofactors, if any, are required for this reaction? H H SCOA1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:a. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What molecule a is required for this reaction to proceed? d. What molecule b is produced in addition to 2? e. What enzyme performs this reaction?
- 1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)Rearrange the following terms to show the process of enzymatic reaction. Use and + to complete the equation. enzyme enzyme-substrate complex enzyme product substrate Several important things should be noted about this reaction: 1. A/an because of the fit between their structures; 2. As a result, something happens to the example, it might be split in two at a particular location. 3. Then the and 4. The enzyme is again. 5. Note that the arrows in the formula for enzyme reaction point acts on a specific to form a/an molecule. For comes apart, yielding the in the reaction and is now free to react _- This means that the reaction is 6. An enzyme-substrate complex can simply go back to the the 7. The products of an enzymatic reaction can react with the enzyme to form the and again; 8. It, in turn, may again form the 9. Therefore, the same. and the may act to cause a to go either way.12. Nirogenase is an enzyme that converts the remarkably stable triple bond in N2 into a usable form. It uses an iron sulfur cluster comprised of iron and the sulfur atoms of several active site cysteine residues. Based on your knowledge of Biochemistry what is the enzyme doing to effectively carry out this reaction? a) stabilizing the transition state for the reaction by hydrophobic effects b) stabilizing the ground state for the reaction by hydrophobic effects c) stabilizing the transition state for the reaction by metal ion catalysis d) stabilizing the ground state for the reaction by metal ion catalysis e) all of the above
- 3. Consider the reaction: H3C-(CH₂) H H C—C—C—SCOA HH H₂C-(CH₂) a. What kind of reaction is being performed here? b. What enzyme performs this reaction? -C—C—C—SCOA H H c. What cofactors, if any, are required for this reaction?21. You want to maintain pH = 7.0 for an enzyme-catalyzed reaction that will produce hydrogen ions along with the desired product. At equal concentrations, which weak acid, if any, will serve as the better buffer for the reaction: acid A, with pk₁= 6.5, or acid B, with pk=7.5? A) acid A B) Water is as good as either of the acids available. C) acid B D) Both are equally effective.5. Examine the graphic below and answer the questions about the enzyme we reviewed in lecture. 1.0 0.01 mM Vo Vmax ATP 1 mM ATP 0.5 1 mM ATP + 0.1 mM AMP 1 [Fru-6-P] (mM) 2 A) What enzyme is this? What reaction does it perform? Of what metabolic pathway is this enzyme a part? B) What allosteric regulator, shown on the graph as presented here, is considered to be a homotropic allosteric factor? C) Which allosteric regulator, shown on the graph as presented here, has the greatest influence on this enzyme? Explain the reasoning behind your answer. D) Name a positive allosteric effector of this enzyme NOT shown on the graph as presented here. What is the origin of this positive allosteric effector...that is, where is it coming from? E) Name a negative allosteric effector of this enzyme NOT shown on the graph as presented here. What is the origin of this negative allosteric effector...that is, where is it coming from? F) Explain how the regulation of this enzyme is tied to the "energy…
