Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.3.2 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)

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

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
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
-
?