ENZYME KINETICS A MODERN APPROACH – PART 4 pptx
ENZYME KINETICS A MODERN APPROACH – PART 4 pptx
... 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 by Fumarase at variousSubstrate Concentrations a Velocity ... phenomenological irreversible inhibition mechanisms arediscussed in turn.APPLICATIONS 67TABLE 4. 3 Estimates of the Catalytic Parameters for the Fumarase-Catalyzedhydration of Fumarate to Malate a V∗max (a. u.) ... exp−kt)(5 .42 )To obtain estimates of Kiand ki,akversus [I0] data set at a fixedsubstrate concentration has to be created. A plot of these kversus [I0]data would yield a rectangular hyperbola...
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ENZYME KINETICS A MODERN APPROACH – PART 2 pptx
... 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 ... important to reiteratethat this treatment applies only for cases where the heat capacities of thereactants and products are equal and temperature independent.Enthalpy changes are related to changes...
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ENZYME KINETICS A MODERN APPROACH – PART 5 pptx
... ternary enzyme substrate complexesEAB (KABand KBA), and the enzyme mass balance are, respectively,v = kcat[EAB] (7.7)K A s=[E] [A] [EA]KBs=[E][B][EB](7.8)KBA=[EB] [A] [EBA]KAB=[EA][B][EAB][ET] ... constant,Eq. (7.11) can be expressed 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 ... 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....
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ENZYME KINETICS A MODERN APPROACH – PART 6 pptx
... Axbecomes greater than that of the 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 ... 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
... service, call 1-800-CALL-WILEY.Library of Congress Cataloging-in-Publication Data:Marangoni, Alejandro G., 1965- Enzyme kinetics : a modern approach / Alejandro G. Marangoni.p. ; cm.ISBN 0 -47 1-15985-9 ... 281.6.1.2 Least-Squares Minimization(Regression Analysis) / 291.6.2 Exact Analytical Solution(Non-Steady-State Approximation) / 391.6.3 Exact Analytical Solution (Steady-StateApproximation) / 40 2 ... Order of a Reaction / 31.2.3 Rate Constant / 4 1.2 .4 Integrated Rate Equations / 4 1.2 .4. 1 Zero-Order Integrated RateEquation / 4 1.2 .4. 2 First-Order Integrated RateEquation / 51.2 .4. 3 Second-Order...
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ENZYME KINETICS A MODERN APPROACH – PART 3 pps
... statistic:χ2=ni=1(yi−ˆyi)2s2i=ni=1wi(yi−ˆyi)2(1.125)Consider a typical experiment where the value of a dependent variable ismeasured several times at a particular value of the independent variable.From these repeated determinations, a mean and variance ... 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 ... not be assumed for the 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...
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ENZYME KINETICS A MODERN APPROACH – PART 7 ppsx
... 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 ... stability, enzyme solutions areincubated at a particular temperature and aliquots removed at the appro-priate times. Enzyme activity in these samples is then measured at the enzyme s temperature ... by an enzyme s normal catalyticpathway to form a stable covalent enzyme inhibitor intermediate, suchas an acyl -enzyme in the case of serine proteases, where the complex isessentially trapped...
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ENZYME KINETICS A MODERN APPROACH – PART 8 ppt
... Loughran,and M. D. Walkinshaw, J. Biol. Chem. 2 74, 249 0 1–2 49 05 (1999).Vilain, A C., V. Okochi, I. Vergely, M. Reboud-Raveax, J P. Mazalelyrat, andM. Wakselman, Biochim. Biophys. Acta 1076, 40 1 4 05 ... Finer-Moore, Y. Wataya, and D. V. Santi,Biochemistry 33, 1508 6–1 50 94 (19 94) .Groutas, W. C., R. Kuang, R. Venkataraman, J. B. Epp, S. Ruan, and O. Prakash,Biochemistry 36, 47 3 9 4 750 (1997).Groutas, W. ... Thepartition ratio was also determined from the ratio of rates: k3/k 4 = 1.5.That the inactivation was active-site directed was also established inseveral ways. As mentioned above, the pK a values...
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ENZYME KINETICS A MODERN APPROACH – PART 9 docx
... less 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, ... Wild-Type,Lys36pArg, and Lys36pMet Trx-PG at 14 ◦C determined with the Synthetic PeptideSubstrate Lysine–Proline–Alanine– Glutamic Acid– Phenylalanine–Phenylalanine(NO2)–Alanine–Leucine a First-Order Rate ... mean of a minimum of two determi-nations ± standard deviation.bss1, substrate consisting of the peptide lysine–proline–alanine–glutamic acid–phenylalanine–phenylalanine (NO2)–alanine–leucine.css2,...
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ENZYME KINETICS A MODERN APPROACH – PART 10 pps
... 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 59models of, 4 8–5 2pH dependence of, 7 9–8 9practical example of enzyme, 5 3–5 8Catalysts, enzymes as, 4 1 4 3Catalytic ... enzymes, 14 0–1 57, 20 5–2 12Standard-state enthalpy of denaturation, 14 7–1 50, 155Standard-state entropy of denaturation, 14 7–1 50, 155Standard-state free energy of denaturation, 14 7–1 50Standard-state ... denaturation, 14 7–1 50, 155Standard-state entropy of denaturation, 14 7–1 50, 155Standard-state free energy of denaturation, 14 7–1 50Standard-state free-energy change (G◦), 14, 24 Steady-state approximations,...
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