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Literature summary for 4.3.3.7 extracted from

  • Karsten, W.E.
    Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine (1997), Biochemistry, 36, 1730-1739.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3-fluoro-2-oxopropanoate
-
Escherichia coli
dipicolinic acid
-
Escherichia coli
L-lysine
-
Escherichia coli
Succinic semialdehyde
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Storage Stability

Storage Stability Organism
-20°C, 10 mM triethanolamine buffer, pH 7.5, 10 mM 2-mercaptoethanol, stable for at least 6 months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate-4-semialdehyde + pyruvate
-
Escherichia coli dihydrodipicolinate + H2O
-
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