ENZYME KINETICS A MODERN APPROACH – PART 2 pptx

... 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 ... constant, and only k 2 and k 3 floated. After preliminary parameter estimates are obtained in this fashion, these parameters should be fixed as constants and the remaining parameters estimat...

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... is appropriate. When more than two values are compared, a one-way analysis of variance (ANOVA), TABLE 4 .2 Rate of Hydration of Fumarate to Malate by Fumarase at various Substrate Concentrations a Velocity ... phenomenological irreversible inhibition mechanisms are discussed in turn. APPLICATIONS 67 TABLE 4.3 Estimates of the Catalytic Parameters for the Fumarase-Catalyzed hydration of F...

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... enzyme substrate complex EAB (K AB ), and the enzyme mass balance are, respectively, v = k cat [EAB] (7 .21 ) K A s = [E] [A] [EA] K AB = [EA][B] [EAB] (7 .22 ) [E T ] = [E] + [EA] + [EAB] (7 .23 ) Normalization ... as v V  max = [B] K  + [B] (7. 12) where V  max = V max [A] K BA + [A] (7.13) and K  = K A s K AB + K AB [A] K BA + [A] = K AB (K A s + [A] ) K BA + [A] (7.1...

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... exponential term, and the shape of the curve approaches that of a straight line. Valuable information can be gained 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 catalyzed by an interfacial enzyme. As the enzyme interface dissociation constant incre...

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... 28 1.6.1.1 Numerical Integration / 28 1.6.1 .2 Least-Squares Minimization (Regression Analysis) / 29 1.6 .2 Exact Analytical Solution (Non-Steady-State Approximation) / 39 1.6.3 Exact Analytical ... customer service, call 1-800-CALL-WILEY. Library of Congress Cataloging-in-Publication Data: Marangoni, Alejandro G., 1965- Enzyme kinetics : a modern approach / Alejandro G. Mar...

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... derivation of an enzyme catalysis model. A steady-state approximation can also be used to obtain the rate equation for an enzyme- catalyzed reaction. 3 .2. 2 Steady-State Model The main assumption made in ... scattered randomly about zero. A large positive value of the SCC is indicative of a systematic deviation of the model from the data. PRACTICAL EXAMPLE 55 TABLE 3 .2 Average and...

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... major subclasses of mechanism-based inhibition. Alternate substrates are processed by an enzyme s normal catalytic pathway to form a stable covalent enzyme inhibitor intermediate, such as an acyl -enzyme ... enzyme A. 12. 3 .2 Kinetic Characterization of Stability Decreases in the activity of an enzyme as a function of time, at dif- ferent temperatures, are shown in Table 12. 2...

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... Groutas et al., 1998; Macchia et al., 20 00; Clemente et al., 20 01). Amino acid analysis of both native and inactivated enzyme can identify which amino acid is modified (for examples see Pochet et al., ... k on and K i of 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 turnove...

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... lysine–proline–alanine–glutamic acid–phenylalanine– phenylalanine (NO 2 )–alanine–leucine. c ss2, substrate consisting of the peptide leucine–serine–phenylalanine (NO 2 )–norleucine–leucine– methyl ... mean of a minimum of two deter- minations ± standard deviation. b ss1, substrate consisting of the peptide lysine–proline–alanine–glutamic acid–phenylalanine– phenylalanine (NO 2 )–alan...

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... INDEX Abbreviations, table for mutation research, 21 4 2 16 Absolute reaction rate theory, 2 3 2 6 Acid–base catalysis, 2 0 2 3 Acidity constant (K a ), 2 0 2 1 Activation, 103 Activation curves, 20 0 2 02. ... entries acid–base, 2 0 2 3 enzyme, 4 1–4 3, 4 8–5 2, 5 2 5 3 in mechanism-based inhibition, 15 8–1 59 models of, 4 8–5 2 pH dependence of, 7 9–8 9 practical e...

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