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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Biochemists working with isolated mitochondria recognize five
energy "states" of mitochondria, depending on the presence or
absence of essential substrates for respiration-O, ADP, oxidizable
substrates, and so forth. The characteristics of each state are:
state 1: mitochondria alone (in buffer containing P;)
state 2: mitochondria + substrate, but respiration low due to
lack of ADP
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…
Chapter 23 Solutions
Biochemistry
Ch. 23 - Prob. 1PCh. 23 - Determining the Amount of ATP Produced from Fatty...Ch. 23 - Prob. 3PCh. 23 - Examining the Labeling of Glucose from 14C.labeled...Ch. 23 - Prob. 5PCh. 23 - Prob. 6PCh. 23 - Prob. 7PCh. 23 - Prob. 8PCh. 23 - Prob. 9PCh. 23 - Prob. 10P
Ch. 23 - Prob. 11PCh. 23 - Understanding Human Energy Consumption During...Ch. 23 - Prob. 13PCh. 23 - Prob. 14PCh. 23 - Prob. 15PCh. 23 - Extending the Mechanism of Methylmalonyl-CoA...Ch. 23 - Prob. 17PCh. 23 - Prob. 18PCh. 23 - Prob. 19PCh. 23 - Understanding a Ubiquitous Series of Metabolic...Ch. 23 - Using the ActiveModel for enoyl-CoA dehydratase,...
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