. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter10: From Proteins To Phenotypes
Section: Chapter Questions
Problem 14QP: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of...
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Question
![. The allosterically regulated enzyme ATCase binds aspartic acid as a
substrate and acylates the a-amino group. Succinate acts as a competitive
inhibitor of ATCase because it binds the active site but can't be acylated. The
dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the
accompanying figure. Panel (b) shows the effect of increasing [succinate]
on v, when [Asp] is held at a low concentration (see thick vertical arrow in
panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see
thin horizontal arrow). Explain the shape of the curve in panel (b). Why
does v, increase initially, before decreasing at higher [succinate]?
Co0-
COO
CH2
CH,
HC -NH,
CH,
COO
COO
Asp
Succinate
[Asp)
[Succinate]
[Asp] in
experiment b
(a)
(b)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F3c36674e-3e5a-40fc-95de-e6a1a68d321e%2Fed8c7b17-29d3-4655-a01d-dd7d6262794d%2F6vh9lw_processed.png&w=3840&q=75)
Transcribed Image Text:. The allosterically regulated enzyme ATCase binds aspartic acid as a
substrate and acylates the a-amino group. Succinate acts as a competitive
inhibitor of ATCase because it binds the active site but can't be acylated. The
dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the
accompanying figure. Panel (b) shows the effect of increasing [succinate]
on v, when [Asp] is held at a low concentration (see thick vertical arrow in
panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see
thin horizontal arrow). Explain the shape of the curve in panel (b). Why
does v, increase initially, before decreasing at higher [succinate]?
Co0-
COO
CH2
CH,
HC -NH,
CH,
COO
COO
Asp
Succinate
[Asp)
[Succinate]
[Asp] in
experiment b
(a)
(b)
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