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Literature summary for 2.1.3.2 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)

Crystallization (Comment) Organism
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)

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 P0A786
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme 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
-
?