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Literature summary for 4.3.1.1 extracted from

  • Karsten, W.E.; Viola, R.E.
    Kinetic studies of L-aspartase from Escherichia coli: pH-dependent activity changes (1991), Arch. Biochem. Biophys., 287, 60-67.
    View publication on PubMed
Search for more literature for 4.3.1.1

Inhibitors

Inhibitors Comment Organism Structure
3-nitropropionate competitive Escherichia coli
dimethyl sulfoxide nonspecific Escherichia coli
DL-2-amino-4-phosphonobutyrate competitive Escherichia coli
ethanol moderate, nonspecific Escherichia coli
methanol moderate, nonspecific Escherichia coli
additional information
-
 Escherichia coli
succinate competitive Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Escherichia coli
Mg2+
-
 Escherichia coli
Mg2+
-
 Hafnia alvei
additional information
-
 Hafnia alvei
additional information absolute requirement for divalent metal ion at high pH value Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Hafnia alvei
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate = fumarate + NH3 mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + hydroxylamine fumarate Escherichia coli ?
-
 ?
L-aspartate r Escherichia coli fumarate + NH3
-
 ?
L-aspartate r Hafnia alvei fumarate + NH3
-
 ?
L-aspartate natural substrate Escherichia coli fumarate + NH3
-
 ?
L-aspartate natural substrate Hafnia alvei fumarate + NH3
-
 ?
additional information
-
 Escherichia coli ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
-
 Escherichia coli