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Literature summary for 2.1.3.2 extracted from

  • Coudray, L.; Kantrowitz, E.R.; Montchamp, J.L.
    Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase (2009), Bioorg. Med. Chem. Lett., 19, 900-902.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
(2S)-2-(([hydroxy(hydroxymethyl)phosphoryl]acetyl)amino)butanedioic acid competitive Escherichia coli
(2S)-2-(([hydroxy(oxido)-lambda5-phosphanyl]acetyl)amino)butanedioic acid competitive Escherichia coli
N-phosphonoacetyl-L-aspartate competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
 Carbamoyl phosphate
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carbamoyl phosphate + L-aspartate
-
 Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000016
-
 N-phosphonoacetyl-L-aspartate
-
 Escherichia coli
0.000193
-
 (2S)-2-(([hydroxy(hydroxymethyl)phosphoryl]acetyl)amino)butanedioic acid
-
 Escherichia coli
0.000417
-
 (2S)-2-(([hydroxy(oxido)-lambda5-phosphanyl]acetyl)amino)butanedioic acid
-
 Escherichia coli