a. A majority of this precursor is used by the enzyme chorismate mutase to synthesize another precursor that is used to make phenylalanine or tyrosine. Experimental data shows that when there is a high concentration of phenylalanine in a cell, more tryptophan is produced. This data also suggests that phenylalanine binds to chorismate mutase but does not bind to the enzyme's active site. Use what we learned in class to describe how this binding could regulate chorismate mutase's activity and result in more tryptophan being produced. b. The common precursor is also a substrate for a second enzyme, anthranilate synthase. The product of that reaction is a precursor for tryptophan. Based on the effect of high concentrations of phenylalanine on chorismate mutase, propose a possible effect of tryptophan on anthranilate synthase. c. How do the regulatory schemes described in parts (a) and (b) allow the cell to maintain the correct ratio of phenylalanine/tyrosine to tryptophan in the cell?
a. A majority of this precursor is used by the enzyme chorismate mutase to synthesize another precursor that is used to make phenylalanine or tyrosine. Experimental data shows that when there is a high concentration of phenylalanine in a cell, more tryptophan is produced. This data also suggests that phenylalanine binds to chorismate mutase but does not bind to the enzyme's active site. Use what we learned in class to describe how this binding could regulate chorismate mutase's activity and result in more tryptophan being produced. b. The common precursor is also a substrate for a second enzyme, anthranilate synthase. The product of that reaction is a precursor for tryptophan. Based on the effect of high concentrations of phenylalanine on chorismate mutase, propose a possible effect of tryptophan on anthranilate synthase. c. How do the regulatory schemes described in parts (a) and (b) allow the cell to maintain the correct ratio of phenylalanine/tyrosine to tryptophan in the cell?
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Transcribed Image Text:9. Bacteria can synthesize tryptophan, tyrosine, and phenylalanine through a series of biochemical
reactions. All three amino acids are derived from the same precursor molecule, as shown in the diagram
below.
OH
но
OH
Common Precursor
Anthranilate
Chorismate
Synthase
Mutase
OH
NH2
00
Trp Precursor
Tyr/Phe Precursor
a. A majority of this precursor is used by the enzyme chorismate mutase to synthesize another
precursor that is used to make phenylalanine or tyrosine. Experimental data shows that when there is a
high concentration of phenylalanine in a cell, more tryptophan is produced. This data also suggests that
phenylalanine binds to chorismate mutase but does not bind to the enzyme's active site. Use what we
learned in class to describe how this binding could regulate chorismate mutase's activity and result in
more tryptophan being produced.
b. The common precursor is also a substrate for a second enzyme, anthranilate synthase. The product
of that reaction is a precursor for tryptophan. Based on the effect of high concentrations of
phenylalanine on chorismate mutase, propose a possible effect of tryptophan on anthranilate synthase.
c. How do the regulatory schemes described in parts (a) and (b) allow the cell to maintain the correct
ratio of phenylalanine/tyrosine to tryptophan in the cell?
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