What compound(s) were the most effective inhibitors and what compound(s) were the most effective activators?

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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What compound(s) were the most effective inhibitors and what compound(s) were the most effective activators?

Aspartate transcarbamoylase (ATCase) catalyzes an early step in the synthesis of the
pyrimidine nucleotides UTP and CTP. The enzyme catalyzes the condensation of carbamoyl
phosphate and aspartate to form carbamoyl aspartate. The reaction pathway is shown in
Figure 16.1 below. The enzyme has been fairly well characterized. It is known to consist of
six regulatory subunits and six catalytic subunits.
HCO3 + Glutamine + ATP
Carbamoyl phosphate + Aspartate
ATCase
Figure 16.1: Pyrimidine synthetic pathway.
N-carbamoylaspartate
UMP
UTP
CTP
In this case, we examine the properties of ATCase isolated from E. coli to illustrate some of
the important regulatory properties of multi-subunit enzymes. As an early enzyme in a multi-
step pathway, the ATCase reaction is a logical one to regulate the synthesis of pyrimidine
nucleotides. Both purine nucleotides and pyrimidine nucleotides are needed in roughly equal
amounts as substrates for DNA synthesis in rapidly dividing cells. The regulation of the
ATCase enzyme ensures a proper balance of purine and pyrimidine pools in E. coli. The goal
in this case was to identify the cellular metabolites that serve as activators and inhibitors of
ATCase.
Transcribed Image Text:Aspartate transcarbamoylase (ATCase) catalyzes an early step in the synthesis of the pyrimidine nucleotides UTP and CTP. The enzyme catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate. The reaction pathway is shown in Figure 16.1 below. The enzyme has been fairly well characterized. It is known to consist of six regulatory subunits and six catalytic subunits. HCO3 + Glutamine + ATP Carbamoyl phosphate + Aspartate ATCase Figure 16.1: Pyrimidine synthetic pathway. N-carbamoylaspartate UMP UTP CTP In this case, we examine the properties of ATCase isolated from E. coli to illustrate some of the important regulatory properties of multi-subunit enzymes. As an early enzyme in a multi- step pathway, the ATCase reaction is a logical one to regulate the synthesis of pyrimidine nucleotides. Both purine nucleotides and pyrimidine nucleotides are needed in roughly equal amounts as substrates for DNA synthesis in rapidly dividing cells. The regulation of the ATCase enzyme ensures a proper balance of purine and pyrimidine pools in E. coli. The goal in this case was to identify the cellular metabolites that serve as activators and inhibitors of ATCase.
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