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Literature summary extracted from

  • Giorgianni, F.; Beranova, S.; Wesdemiotis, C.; Viola, R.E.
    Mapping the mechanism-based modification sites in L-aspartase from Escherichia coli (1997), Arch. Biochem. Biophys., 341, 329-336.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.1 aspartate beta-semialdehyde
-
 Escherichia coli
4.3.1.1 fumaric acid aldehyde
-
 Escherichia coli
4.3.1.1 fumaric acid aldehyde ethyl ester
-
 Escherichia coli
4.3.1.1 additional information
-
 Escherichia coli
4.3.1.1 o-phospho-D-serine competitive Escherichia coli
4.3.1.1 O-phospho-L-serine competitive Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.1 0.54
-
 L-aspartate C273A mutant, pH 7.0 Escherichia coli
4.3.1.1 0.6
-
 L-aspartate C140S/C273A mutant, pH 7.0 Escherichia coli
4.3.1.1 1.2
-
 L-aspartate wild-type, pH 7.0 Escherichia coli
4.3.1.1 1.3
-
 L-aspartate C273S mutant, pH 7.0 Escherichia coli
4.3.1.1 12
-
 L-aspartate K139I mutant, pH 7.0 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.1 Escherichia coli
-
 C273S, C273A, C140S/C273A, K139I (mutants)
-

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
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.1 30
-
-
 Escherichia coli