BRENDA - Enzyme Database show

Pyruvate-aspartic semialdehyde condensing enzyme (Escherichia coli)

Shedlarski, J.G.; Methods Enzymol. 17B, 129-134 (1971)
No PubMed abstract available

Data extracted from this reference:

General Stability
EC Number
General Stability
Organism
4.3.3.7
repeated freezing/thawing causes loss of activity
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
L-lysine
Ki: 0.21 mM
Escherichia coli
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.13
-
pyruvate
-
Escherichia coli
4.3.3.7
0.25
-
L-aspartate-4-semialdehyde
-
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.3.3.7
cytosol
-
Escherichia coli
5829
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Escherichia coli
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.3.3.7
additional information
-
-
Escherichia coli
Storage Stability
EC Number
Storage Stability
Organism
4.3.3.7
-20°C, 0.06 M phosphate buffer, pH 7.5, 3 months, no loss of activity
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate-4-semialdehyde + pyruvate
-
33907
Escherichia coli
dihydrodipicolinate + H2O
-
33907
Escherichia coli
?
4.3.3.7
additional information
no reaction with oxaloacetic acid, phosphoenolpyruvate, glutamic semialdehyde, N-acetylaspartic semialdehyde, succinic semialdehyde
33907
Escherichia coli
?
-
-
-
-
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.3.3.7
8.4
-
-
Escherichia coli
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.21
-
L-lysine
-
Escherichia coli
General Stability (protein specific)
EC Number
General Stability
Organism
4.3.3.7
repeated freezing/thawing causes loss of activity
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
L-lysine
Ki: 0.21 mM
Escherichia coli
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.3.3.7
0.21
-
L-lysine
-
Escherichia coli
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.3.3.7
0.13
-
pyruvate
-
Escherichia coli
4.3.3.7
0.25
-
L-aspartate-4-semialdehyde
-
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.3.3.7
cytosol
-
Escherichia coli
5829
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.3.3.7
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.3.3.7
additional information
-
-
Escherichia coli
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
4.3.3.7
-20°C, 0.06 M phosphate buffer, pH 7.5, 3 months, no loss of activity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
L-aspartate-4-semialdehyde + pyruvate
-
33907
Escherichia coli
dihydrodipicolinate + H2O
-
33907
Escherichia coli
?
4.3.3.7
additional information
no reaction with oxaloacetic acid, phosphoenolpyruvate, glutamic semialdehyde, N-acetylaspartic semialdehyde, succinic semialdehyde
33907
Escherichia coli
?
-
-
-
-
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.3.3.7
8.4
-
-
Escherichia coli