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The Microbiological Production of Industrial Chemicals,” Scientific American 245 (1981):155–178. Hofstee, B. H. , “Specificity of Esterases: I. Identification of Two Pancreatic Aliesterases,” J. Biol. Chem. 199 (1952):357–364.

9) Substituting Eq. 9) into Eq. 17) CES = k 2 + k3 + CS k1 Substitution of Eq. 17) into Eq. 18) r= P =− S = k2 + k3 + dt dt K C M S + CS k1 which is the same as the Michaelis-Menten equation, Eq. 11), except that the meaning of KM is different. In the Michaelis-Menten approach, KM is Enzyme Kinetics 2-11 equal to the dissociation constant k2/k1, while in the Briggs-Haldane approach, it is equal to (k2 + k3)/k1. Eq. 18) can be simplified to Eq. 11) if k2 % k3, which means that the product-releasing step is much slower than the enzyme-substrate complex dissociation step.

Justify your answer by showing the effect of the inhibitor graphically. [Contributed by Professor Gary F. 20 The effect of an inhibitor on an enzyme reaction was studied by measuring the initial rates at three different initial inhibitor concentrations. 08 5 a. Write the kinetic model for this enzyme reaction. b. Derive the rate equation. State your assumptions for any simplification of the rate equation. c. Estimate the value of inhibition kinetic parameter. 21 An enzyme (cathepsin) hydrolyzes L-glutamyl-L-tyrosine to carbobenzoxy-L-glutamic acid and L-tyrosine.

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Biochemical engineering by James M. Lee

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