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Literature summary extracted from

  • Falzone, C.J.; Karsten, W.E.; Conley, J.D.; Viola, R.E.
    L-Aspartase from Escherichia coli: substrate specificity and role of divalent metal ions (1988), Biochemistry, 27, 9089-9093.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.1 (1-aminopropyl)-phosphonate
-
Escherichia coli
4.3.1.1 (3-aminopropyl)-phosphonate
-
Escherichia coli
4.3.1.1 (aminomethyl)-phosphonate
-
Escherichia coli
4.3.1.1 2-hydroxy-3-nitropropionate
-
Escherichia coli
4.3.1.1 3-nitropropionate
-
Escherichia coli
4.3.1.1 beta-aspartylhydrazine
-
Escherichia coli
4.3.1.1 D-2-methylmalate
-
Escherichia coli
4.3.1.1 D-malate
-
Escherichia coli
4.3.1.1 DL-2-amino-3-phosphonopropionate
-
Escherichia coli
4.3.1.1 DL-2-amino-4-phosphonobutyrate
-
Escherichia coli
4.3.1.1 DL-2-bromosuccinate
-
Escherichia coli
4.3.1.1 L-2-chlorosuccinate
-
Escherichia coli
4.3.1.1 L-malate
-
Escherichia coli
4.3.1.1 Mercaptosuccinate
-
Escherichia coli
4.3.1.1 Methylsuccinate
-
Escherichia coli
4.3.1.1 N-acetyl-L-aspartate
-
Escherichia coli
4.3.1.1 o-phospho-D-serine
-
Escherichia coli
4.3.1.1 Phosphoglycolate
-
Escherichia coli
4.3.1.1 succinate
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.1.1 Ca2+ activates at pH 7.0 Escherichia coli
4.3.1.1 Cd2+ activates at pH 7.0 Escherichia coli
4.3.1.1 Co2+ activates at pH 7.0 Escherichia coli
4.3.1.1 Mg2+
-
Escherichia coli
4.3.1.1 Mn2+ activates at pH 7.0 Escherichia coli
4.3.1.1 additional information
-
Escherichia coli
4.3.1.1 Zn2+ activates at pH 7.0 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.1 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.1 L-aspartate r Escherichia coli fumarate + NH3
-
?
4.3.1.1 L-aspartate absolutely specific Escherichia coli fumarate + NH3
-
?
4.3.1.1 L-aspartate natural substrate Escherichia coli fumarate + NH3
-
?