ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
... cooperativity, which can have noninteger values.Estimates of the parameters kand n are obtained using standard non-linear regression procedures available in most modern graphical softwarepackages. ... asvVmax=[B]K+ [B](7.12)whereVmax=Vmax [A] KBA+ [A] (7.13)andK=K A sKAB+ KAB [A] KBA+ [A] =KAB(K A s+ [A] )KBA+ [A] (7.14)From determinations of Kand Vmaxat ... the mechanism of an enzyme- catalyzed reaction from steady-state kinetic analysis. The determinationof the mechanism of an enzymatic reaction is neither a trivial task nor aneasy task. The...
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ENZYME KINETICS A MODERN APPROACH – PART 2 pptx
... hydroxyl ion–catalyzed reaction, kHAis the rate constantfor the undissociated acid-catalyzed reaction, and k A −is the rate constantfor the conjugate base–catalyzed reaction.32 TOOLS AND TECHNIQUES ... TOOLS AND TECHNIQUES OF KINETIC ANALYSIS1.4 ACID–BASE CHEMICAL CATALYSISMany homogeneous reactions in solution are catalyzed by acids and bases.ABr¨onsted acid is a proton donor,HA + H2O ... for example, the reaction A → B →C. Usually, equations in differential or algebraic form are fitted to indi-vidual data sets, A, B, and C and a set of parameter estimates obtained.26 TOOLS AND...
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ENZYME KINETICS A MODERN APPROACH – PART 4 pptx
... thecomparison of two values, a two-tailed t -test is appropriate. When morethan two values are compared, a one-way analysis of variance (ANOVA),TABLE 4.2 Rate of Hydration of Fumarate to Malate ... V∗maxand K∗scorrespond, respectively, to apparent enzyme maxi-mum velocity and apparent enzyme substrate dissociation constant at a particular pH. For the model above, V∗max= Vmax/α and ... (a. u.)SubstrateConcentration (M) Without Inhibitor With Inhibitor2 .5 × 10 5 3000 2 950 3 050 155 0 150 0 1600 5. 0 × 10 5 4900 4 950 4 850 250 0 255 0 2 450 1.0 × 10−47100 7 050 7 150 3700 3 750 3 650 2.0...
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ENZYME KINETICS A MODERN APPROACH – PART 6 pptx
... exponential term, and the shape of thecurve approaches that of a straight line. Valuable information can begained from analysis of the early and late stages of this reaction.11.2.1 Early Stages ... plot for an interfa-cial enzyme. various parameters in Eq. (10.9) on the velocity of a reaction catalyzedby an interfacial enzyme. As the enzyme interface dissociation constantincreases (i.e., ... DETERMINATION OF SATURATION INTERFACIAL ENZYME COVERAGEThe amount of enzyme required to saturate the substrate interface can bedetermined from a velocity versus [ET]plotatafixedvalueof [A s]. Asthe...
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ENZYME KINETICS A MODERN APPROACH – PART 1 pps
... call 1-800-CALL-WILEY.Library of Congress Cataloging-in-Publication Data:Marangoni, Alejandro G., 19 65- Enzyme kinetics : a modern approach / Alejandro G. Marangoni.p. ; cm.ISBN 0-471- 159 85- 9 ... Vmax /52 3.4 Practical Example / 53 3 .5 Determination of Enzyme Catalytic Parametersfrom the Progress Curve / 58 ENZYME KINETICS A Modern Approach ALEJANDRO G. MARANGONIDepartment of Food ... The law of mass action statesthat the rate at which the reactant A is converted to product C is pro-portional to the number of molecules of A available to participate inthe chemical reaction....
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ENZYME KINETICS A MODERN APPROACH – PART 3 pps
... scattered randomly about zero. A large positive value of theSCC is indicative of a systematic deviation of the model from the data.PRACTICAL EXAMPLE 55 TABLE 3.2 Average and Standard Deviation ... derivationof an enzyme catalysis model. A steady-state approximation can also beused to obtain the rate equation for an enzyme- catalyzed reaction.3.2.2 Steady-State ModelThe main assumption made in ... Exact Analytical Solution (Non-Steady-StateApproximation)Exact analytical solutions for the reaction A → B → C can be obtained bysolving the differential equations using standard mathematical...
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ENZYME KINETICS A MODERN APPROACH – PART 7 ppsx
... reactionTABLE 12.1 Relative Activity of Two Enzymes as a Function of TemperatureTemperature(◦C) Enzyme 1 Enzyme 210 25 10 15 37 .5 15 20 50 20 25 75 25 30 100 30 35 100 50 40 95 75 45 85 ... thekinetic characterization of enzyme stability. 150 CHARACTERIZATION OF ENZYME STABILITYAlternatively, S◦Dcould be calculated from knowledge of G◦Dat a particular temperature and H◦D:S◦D=H◦D− ... treatment above assumes that there are no differences in heat capac-ity between native and denatured states of an enzyme and that the heatcapacity remains constant throughout the temperature...
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ENZYME KINETICS A MODERN APPROACH – PART 8 ppt
... Kiof an alter-nate substrate. Addition of an alternate substrate inhibitor to an enzyme assay results in an exponential decrease in rate to some final steady-state turnover of substrate (Fig. ... 1.7 ±0 .5. Thepartition ratio was also determined from the ratio of rates: k3/k4= 1 .5. That the inactivation was active-site directed was also established inseveral ways. As mentioned above, ... 1978;Fukuwaka et al., 19 85) ].Although the data in Fig. 14.2 may appear to be visually consistent with a rectangular hyperbola pattern (Michaelis–Menten model), it is a rathersimple matter to...
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ENZYME KINETICS A MODERN APPROACH – PART 9 docx
... than either valineand serine mutants, which had comparable catalytic constants. Comparedto valine and serine, alanine has the smallest van der Waals volume andaccessible surface area. Therefore, ... mean of a minimum of two deter-minations ± standard deviation.bss1, substrate consisting of the peptide lysine–proline–alanine–glutamic acid–phenylalanine–phenylalanine (NO2)–alanine–leucine.css2, ... 100%)0 25 50 75 051 0Time (min)(b) 15 20 25 30100Figure 15. 5. Inactivation of amino terminal fragment mutant. Inactivation test of N-frag-ment, N-frag (A) , and N-frag(B) mutants showed that individual...
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ENZYME KINETICS A MODERN APPROACH – PART 10 pps
... enzymes, 14 0–1 57 , 20 5 2 12Standard-state enthalpy of denaturation,14 7–1 50 , 155 Standard-state entropy of denaturation,14 7–1 50 , 155 Standard-state free energy of denaturation,14 7–1 50 Standard-state ... entriesacid–base, 2 0–2 3 enzyme, 4 1–4 3, 4 8 5 2, 5 2 5 3in mechanism-based inhibition, 15 8–1 59 models of, 4 8 5 2pH dependence of, 7 9–8 9practical example of enzyme, 5 3 5 8Catalysts, enzymes as, 4 1–4 3Catalytic ... model, 50 substrate concentration and, 5 1 5 2transient reaction phases and, 129, 134Mean residual analysis, 5 3 5 8Mean residuals, 5 3 5 6Mechanism-based enzyme inhibition, 15 8–1 71described, 15 8–1 59 Michaelis...
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