Kinetics of Enzyme Reactions -Excel sheet for calculations

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Department
Chemical and Biochemical Engineering
Course
Chemical and Biochemical Engineering 2290A/B
Professor
Mita Ray
Semester
Fall

Description
Excelet The Kinetics of Enzyme Reactions Objective: To explore the chemical kinetics of enzyme mediated biochemical reactions. (This is consecutive reactions with equilibrium in the first step.) DEFINE: S E ES P KM (place your cursor over the green cells above) Click on tabs to navigate! There are a total of thirteen (13) tabs !!ote on screen size Start by reviewing some simple chemical kinetics! Solver Add-in and Analysis ToolPak must be loaded! See "needed Add-ins tab!!! Sinex 2008 Review of Chemical Kinetics To be able to understand enzyme kinetics, you must know the basics of chemical kinetics. How does a catalyst work? w/o cat enzyme reactants 1 9 -10 -10 FALSE 2 46.2 -10 -10 activated complex products 3 18.3 -10 -10 50 FALSE 40 30 PE 20 10 without catalyst For more info on PE with catalyst diagrams - reaction coordinate with enzyme How does the concentration of a reactant influence the rate of a chemical reaction? zero first second 0 0 -1 -1 -1 0.1 -1 -1 -1 0.2 -1 -1 -1 e 0.3 -1 -1 -1 / M 0.4 -1 -1 -1 t R 0.5 -1 -1 -1 For more on rates, see the concentration, M Chemical Kinetics Simulation - Sinex 2008 For more on consecutive reactions - Enzyme Kinetics (E) = k = o 0 cat ### Michaelis-Menten equation Select enzyme 2 vmax 1 (- - - -) KM= 1.20E-02 Does this look like any typical reaction? v v (S) o (S) max 0 ### 0 1 ### 2.94E-01 0.01 1 1.00E-02 4.55E-01 locating Km 0.01 1 vo= initial 1.50E-02 5.56E-01 1.2E+0000 0.5 0.02 1 rate of ### 6.25E-01 ### 0.5 0.02 1 reaction ### 6.76E-01 1.0E### 0 0.03 1 This is the ### 7.14E-01 0.03 1 rate at the ### 7.69E-01 8.0E-01 0.04 1 very start ### 8.06E-01 vo 6.0E-01s 0.05 1 of the ### 8.54E-01 scale factor 0.07 1 reaction; 1.00E-01 8.93E-01 4.0E-01 0.10 1 hence the 1.50E-01 9.26E-01 0.15 1 initial rate 2.00E-01 9.43E-01 2.0E-01 0.20 1 at (So . The (S) axis will rescale 0.0E+00 based on the enzyme (S) selected. substrate TRUE TRUE carbon dioxide Enzyme kinetics data follow a hyperbolic path, where they asymptotically approach tmaxs the enzyme becomes saturated. How does the order of the reaction behave? answer Sinex 2008 x-axis enzyme substratekcats ) KM(M) scale factor 1 acetylcholinesterase acetylcholine### ### 1000 2 carbonic anhydrase 1 carbon dioxide### 1.20E-02 10 3 carbonic anhydrase 2 bicarbonate io### 0.03 10 4 catalase hydrogen peroxide ### 1.1 0.5 5 fumarase 1 fumarate ion ### ### 50000 6 fumarase 2 malate ion ### ### 50000 7 triosephopyceraiomhydae3-phosphate ### ### 1000 8 beta-lactamase benzylpenicillin ### ### 10000 data from: http://iftsa.org/outreach/so/tutorials/EnzymeKinetics.pdto link
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