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Literature summary for 4.3.1.1 extracted from

  • Mizuta, K.; Tokushige, M.
    Role of sulfhydryl groups in aspartase from Escherichia coli (1975), Biochim. Biophys. Acta, 403, 221-231.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli
D-Aspartate competitive Escherichia coli
iodoacetamide
-
 Escherichia coli
additional information
-
 Escherichia coli
N-ethylmaleimide
-
 Escherichia coli
p-hydroxymercuribenzoate
-
 Escherichia coli
succinate competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5
-
 L-aspartate native enzyme Escherichia coli
12.5
-
 L-aspartate N-ethylmaleimide-modified enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate natural substrate Escherichia coli fumarate + NH3
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
 Escherichia coli
7.3
-
 N-ethylmaleimide-modified enzyme, in the absence of MgCl2 Escherichia coli
8.2
-
 N-ethylmaleimide-modified enzyme, in the presence of MgCl2 Escherichia coli
8.3
-
 native enzyme in the absence of MgCl2 Escherichia coli
8.8
-
 native enzyme in the presence of MgCl2 Escherichia coli