Literature summary for 2.1.3.2 extracted from

Peterson, A.W.; Cockrell, G.M.; Kantrowitz, E.R.
A second allosteric site in Escherichia coli aspartate transcarbamoylase (2012), Biochemistry, 51, 4776-4778.

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Protein Variants

Protein Variants	Comment	Organism
H20A	the mutation results in the complete loss of synergistic inhibition by UTP	Escherichia coli
K56A	the mutation results in the complete loss of synergistic inhibition by UTP	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
CTP	aspartate transcarbamoylase is feedback inhibited by CTP in the presence of CTP. CTP and UTP do not bind competitively, CTP binding structure, overview	Escherichia coli
UTP	aspartate transcarbamoylase is feedback inhibited by UTP in the presence of CTP. UTP binds to a unique site on each regulatory chain of the enzyme that is near but not overlapping with the known CTP site. CTP and UTP do not bind competitively, UTP binds to the r6 regulatory chain of ATCase, UTP binding structure, overview	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A786	-	-

Synonyms

Synonyms	Comment	Organism
aspartate transcarbamoylase	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	mechanisms of allosteric regulation in aspartate transcarbamoylase, overview	Escherichia coli

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Release 2023.1 (January 2023)