ATP-liganded form of aspartate transcarbamoylase, the logical regulatory target for allosteric control in divergent bacterial systems.
In Escherichia coli, the mechanism for regulatory control of aspartate transcarbamoylase is clear; CTP allosterically inhibits catalysis in direct competition with ATP. However, both CTP and ATP may be activators or may have no effect on aspartate transcarbamoylases from other enteric bacteria. A common regulatory logic observed was that the ATP-activated enzymes were rendered less active as the result of competition with CTP, regardless of the independent effects.
Wild
J R
JR
Department of Biochemistry and Biophysics, Texas A & M University System, College Station 77843.
Johnson
J L
JL
Loughrey
S J
SJ
D000255:Adenosine Triphosphate / Q000502:physiology*; D000494:Allosteric Regulation; D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D002384:Catalysis; D003570:Cytidine Triphosphate / Q000502:physiology*; D003597:Cytosine Nucleotides / Q000502:physiology*; D004755:Enterobacteriaceae / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*
D003597:Cytosine Nucleotides; D003570:Cytidine Triphosphate; D000255:Adenosine Triphosphate; D001221:Aspartate Carbamoyltransferase