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Literature summary extracted from

  • Alam, N.; Stieglitz, K.A.; Caban, M.D.; Gourinath, S.; Tsuruta, H.; Kantrowitz, E.R.
    240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase (2004), J. Biol. Chem., 279, 23302-23310.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.2 mutant K244N, loss of numerous local T-state stabilizing interactions Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.2 K244A dramatic reduction in homotropic cooperativity and the ability of heterotropic effectors to modulate activity Escherichia coli
2.1.3.2 K244N dramatic reduction in homotropic cooperativity and the ability of heterotropic effectors to modulate activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 4
-
 L-aspartate mutant K244N, pH 8.3, 25°C Escherichia coli
2.1.3.2 8.4
-
 L-aspartate mutant K244A, pH 8.3, 25°C Escherichia coli
2.1.3.2 12.4
-
 L-aspartate wild-type, pH 8.3, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.2 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
-
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