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Literature summary for 2.1.3.2 extracted from

  • Rabinowitz, J.D.; Hsiao, J.J.; Gryncel, K.R.; Kantrowitz, E.R.; Feng, X.J.; Li, G.; Rabitz, H.
    Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase (2008), Biochemistry, 47, 5881-5888.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
ATP ATP enhances ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations) Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
CTP CTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations) Escherichia coli
GTP GTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations) Escherichia coli
UTP UTP inhibits ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Synonyms

Synonyms Comment Organism
aspartate transcarbamoylase
-
 Escherichia coli
ATCase
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 Escherichia coli