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Literature summary for 4.3.3.7 extracted from

  • Shedlarski, J.G.
    Pyruvate-aspartic semialdehyde condensing enzyme (Escherichia coli) (1971), Methods Enzymol., 17B, 129-134.
No PubMed abstract available

General Stability

General Stability Organism
repeated freezing/thawing causes loss of activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-lysine Ki: 0.21 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
pyruvate
-
Escherichia coli
0.25
-
L-aspartate-4-semialdehyde
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Escherichia coli 5829
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, 0.06 M phosphate buffer, pH 7.5, 3 months, no loss of activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate-4-semialdehyde + pyruvate
-
Escherichia coli dihydrodipicolinate + H2O
-
?
additional information no reaction with oxaloacetic acid, phosphoenolpyruvate, glutamic semialdehyde, N-acetylaspartic semialdehyde, succinic semialdehyde Escherichia coli ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.21
-
L-lysine
-
Escherichia coli