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

BRENDA support

Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.2 2.3
-
 L-aspartate C47A/A241C mutant enzyme 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
-
-
-

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
-
 ?