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Literature summary for 2.1.3.2 extracted from

  • Baker, D.P.; Aucoin, J.M.; Williams, M.K.; DeMello, L.A.; Kantrowitz, E.R.
    Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis (1995), Protein Expr. Purif., 6, 679-684.
    View publication on PubMed
Search for more literature for 2.1.3.2

Activating Compound

Activating Compound Comment Organism Structure
acetate 25 mM, 2.3fold activation Bacillus subtilis
additional information activity is not regulated by nucleotide triphosphates Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
additional information
-
 additional information enzyme exhibits Michaelis-Menten kinetics for both of its substrates Bacillus subtilis
0.11
-
 Carbamoyl phosphate
-
 Bacillus subtilis
7
-
 aspartate
-
 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
 6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme Escherichia coli
33000
-
 6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose, Matrex gel Red A, Matrex Phenyl Cellufine Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
148.3
-
 recombinant enzyme Bacillus subtilis
333
-
 recombinant enzyme, in the presence of 50 mM Tris-acetate Bacillus subtilis

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dodecamer 6 * 33000 + 6 * 17000, 2C3/3R2 holoenzyme Escherichia coli