Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 23, Problem 18P
Interpretation Introduction

Interpretation:

The components of multi-functional enzyme cooperate to carry or channel the acyl-CoA substrate from one active site to the next in a cycle fashion needs to be described.

Concept Introduction:

Many enzymes in biochemical pathways are assembled into multifunctional enzyme complexes. The successive enzymatic reactions proceed transferring the intermediates between individual enzymes in the enzyme complex without diffusing into aqueous medium. This mode is known as channeling mechanism. In particular, enzymes in fatty acid synthesis and ß oxidation form multifunctional enzyme complexes to achieve kinetic advantages.

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not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…
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