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Literature summary for 2.1.3.2 extracted from

  • Jin, L.; Stec, B.; Lipscomb, W.N.; Kantrowitz, E.R.
    Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1.ANG (1999), Proteins Struct. Funct. Genet., 37, 729-742.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
P268A 40fold reduction in activity, concentration of N-(phosphonoacetyl)-L-aspartate for maximal activation is increased 233fold as compared to the wild-type, less activation by ATP, stronger inhibition by CTP Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information sigmoidal saturation curve for aspartate Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carbamoylphosphate + L-aspartate Escherichia coli
-
phosphate + N-carbamoyl-L-aspartate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
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
-
?
carbamoylphosphate + L-aspartate
-
Escherichia coli phosphate + N-carbamoyl-L-aspartate
-
?

Subunits

Subunits Comment Organism
More holoenzyme is a dodecamer composed of 2 catalytic trimers and 3 regulatory dimers, the catalytic chain is composed of 2 structural domains, the aspartate domain and the carbamoylphosphate domain which are involved in the binding of aspartate and carbamoylphosphate respectively, the regulatory chain is also composed of 2 domains, the allosteric and the zinc domains, which are involved in the binding of allosteric effectors and zinc Escherichia coli