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

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.1 5,5'-dithiobis(2-nitrobenzoate)
-
 Escherichia coli
4.3.1.1 D-Aspartate competitive Escherichia coli
4.3.1.1 iodoacetamide
-
 Escherichia coli
4.3.1.1 additional information
-
 Escherichia coli
4.3.1.1 N-ethylmaleimide
-
 Escherichia coli
4.3.1.1 p-hydroxymercuribenzoate
-
 Escherichia coli
4.3.1.1 succinate competitive Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.1 2.5
-
 L-aspartate native enzyme Escherichia coli
4.3.1.1 12.5
-
 L-aspartate N-ethylmaleimide-modified enzyme 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 natural substrate Escherichia coli fumarate + NH3
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.1 additional information
-
-
 Escherichia coli
4.3.1.1 7.3
-
 N-ethylmaleimide-modified enzyme, in the absence of MgCl2 Escherichia coli
4.3.1.1 8.2
-
 N-ethylmaleimide-modified enzyme, in the presence of MgCl2 Escherichia coli
4.3.1.1 8.3
-
 native enzyme in the absence of MgCl2 Escherichia coli
4.3.1.1 8.8
-
 native enzyme in the presence of MgCl2 Escherichia coli