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Literature summary for 2.5.1.72 extracted from

  • Ceciliani, F.; Caramori, T.; Ronchi, S.; Tedeschi, G.; Mortarino, M.; Galizzi, A.
    Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase (2000), Protein Expr. Purif., 18, 64-70.
    View publication on PubMed

Application

Application Comment Organism
synthesis production of quinolinic acid from L-aspartate, dihydroxyacetone phosphate, and O2 by use of enzymes NadA and NadB Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38240
-
x * 38246, mass spectrometry, x * 38240, calculated Escherichia coli
38246
-
x * 38246, mass spectrometry, x * 38240, calculated Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
isoform NadA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme, purification from inclusion bodies Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
continuous assay method Escherichia coli
0.6
-
pH 7.0, 25°C Escherichia coli

Subunits

Subunits Comment Organism
? x * 38246, mass spectrometry, x * 38240, calculated Escherichia coli

Synonyms

Synonyms Comment Organism
quinolinate synthetase
-
Escherichia coli