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Literature summary 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)

EC Number Cloned (Comment) Organism
4.3.3.7
-
Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 3-fluoro-2-oxopropanoate
-
Escherichia coli
4.3.3.7 dipicolinic acid
-
Escherichia coli
4.3.3.7 L-lysine
-
Escherichia coli
4.3.3.7 Succinic semialdehyde
-
Escherichia coli

KM Value [mM]

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

Organism

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

Storage Stability

EC Number Storage Stability Organism
4.3.3.7 -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)

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