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

BRENDA support

Literature summary for 2.1.3.2 extracted from

  • Mort, J.S.; Chan, W.W.C.
    Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits (1975), J. Biol. Chem., 250, 653-660.
    View publication on PubMed
Search for more literature for 2.1.3.2

Inhibitors

Inhibitors Comment Organism Structure
aspartate
-
 Escherichia coli
CTP competitive vs. carbamoyl phosphate Escherichia coli
L-aspartate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.9
-
 L-aspartate complex of catalytic and regulatory subunits, C3R6 Escherichia coli
44.7
-
 L-aspartate complex of catalytic subunits, C3 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
-
 ?

Subunits

Subunits Comment Organism
More characterization of a complex between catalytical and regulatory subunit Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
7.9
-
 L-aspartate substrate inhibition, complex of catalytic and regulatory subunits, C3R6 Escherichia coli
80
-
 aspartate substrate inhibition, complex of catalytic subunits, C3 Escherichia coli