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Literature summary extracted from

  • Endrizzi, J.A.; Beernink, P.T.; Alber, T.; Schachman, H.K.
    Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation (2000), Proc. Natl. Acad. Sci. USA, 97, 5077-5082.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 cocrystallization of catalytic subunit with N-(phosphonoacetyl)-L-aspartate by vapor diffusion, crystals grow from 0.005 ml of 100 mM Tris-HCl, pH 6.8, 20 mM calcium acetate, 5.8% polyethylene glycol 8000 and 0.005 ml of catalytic subunit in 10 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol and 2 mM N-(phosphonoacetyl)-L-aspartate Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 Escherichia coli P0A786
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.2 recombinant His6-tagged enzyme Escherichia coli

Substrates and Products (Substrate)

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