The following experimental data were collectedduring a study of the catalytic activity of an intestinal peptidase with the substrateglycylglycine:Glycylglycine + H2O → 2 glycine[S] (mM)Product formed (µmol/min¬1)0.210.240.281.52.03.04.00.330.408.016.00.45Use graphical analysis (see Box 6-1) to determine the Vmax and Km for this enzymepreparation and substrate.

Vmax is the maximum rate of enzyme catalysis when the enzyme is saturated by the substrate or…

Answered: The following experimental data were…

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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From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
What is the principle of LAP? Question 3 options: A) phosphatase activity liberates naphthol and immediately coupled with a diazonium salt which forms an insoluble, visible pigment at sites of phosphatase activity B) naphthol couples with fast garnet and forms insoluble maroon deposits at sites of enzyme activity C) peroxidase present in the primary granules of the granulocytic line transfers hydrogen from various dye substrates to hydrogen peroxidase which yields a colored derivative of the dye which is localized at the site of the enzyme activity D) ferric iron deposits in tissue (present mostly as ferric iron within the storage proteinferritin) then react with the soluble ferrocyanide in the stain
The O2-consumption curve of a dilute, well-buff ered suspension of mito chondria containing an excess of ADP and Pi takes the following form: Sketch the curves obtained when (a) amytal is added at time t = 1 and (b) amytal is added at t = 1 and succinate is added at t = 2.
Neuraminidase (NA) catalyzes a hydrolysis of the glycosidic linkages of sialic acids using a mechanism shown in Fig. (a). and Fig. (b) shows competitive inhibitors of NA Considering the mechanism of NA, why do zanamivir and oseltamivir inhibit NA so potently?
Aconitase catalyzes the conversion of Citrate to Isocitrate in the TCA cycle. The standard free energy change (AG°) for this reaction is +6.7 kJ/mol. The observed free energy change (AG) for the reaction in pig heart mitochondria is +0.8 kJ/mol. The ratio of [isocitrate]/[citrate] in these mitochondria is: Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 10 b. 1 100 0.01 e f 0.33 0.10 h 0.25 i 2
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? 0.125 mM 0.25 mM 0.50 mM 1.25 mM 5.0 mM
Which of the following statements are False?
The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL Also, the molar mass of the olive oil is 885 g/mol. If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?
Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D
Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹
There are three different types of SOD enzymes in the human body named SODI, SOD2 and SOD3. The most important is SOD1. b. (i) Describe the structure of SOD1. (ii) Describe the active site of this enzyme clearly indicating the metal ions involved, their coordination numbers, the geometry around the metal ions and the names of the amino acids directly coordinated to these metal ions. (iii) What is the role of each metal ion? (iv) Draw and explain the catalytic cycle for the conversion of the superoxide anion.

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