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Literature summary for 2.1.3.2 extracted from

  • West, J.M.; Tsuruta, H.; Kantrowitz, E.R.
    Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation (2002), J. Biol. Chem., 277, 47300-47304.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A241C reduced affinity for aspartate, hyperbolic aspartate saturation curve Escherichia coli
C47A Hill coefficient 1.3 as compared to 2.4 for wild-type Escherichia coli
C47A/A241C non-reducing conditions, reduced affinity for aspartate, hyperbolic aspartate saturation curve Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3
-
L-aspartate C47A/A241C mutant enzyme 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
-
-
-

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
-
?