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Literature summary extracted from

  • Gardner, P.R.; Fridovich, I.
    Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis (1991), Arch. Biochem. Biophys., 284, 106-111.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.72 1,10-phenanthroline inhibits reactivation of O2-inactivated enzyme Escherichia coli
2.5.1.72 2,2'-dipyridyl inhibits reactivation of O2-inactivated enzyme Escherichia coli
2.5.1.72 H2O2 1 mM, inactivation Escherichia coli
2.5.1.72 O2 the activity of the enzyme within Escherichia coli is diminished by exposure of the cells to 4.2 atm O2, while the activity in extracts is rapidly decreased by 0.2 atm O2. Inactivation in extracts can be gradually reversed during anaerobic incubation, but is blocked by alpha, alpha'-dipyridyl or by 1,10-phenanthroline Escherichia coli
2.5.1.72 paraquat inactivation Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.72 Iron sequence contains a Cys-W-X-Cys-Y-Z-Cys sequence characteristic for (Fe-S)4-containing proteins. Enzyme is inhibited by Fe(II)-chelating agents Escherichia coli

Organism

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.5.1.72 O2-dependent inactivation inactivation in extracts can be gradually reversed during anaerobic incubation, but is blocked by 2,2'-dipyridyl or by 1,10-phenanthroline Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.72 iron-sulfur centre sequence contains a Cys-W-X-Cys-Y-Z-Cys sequence characteristic for (Fe-S)4-containing proteins. Enzyme is inhibited by Fe(II)-chelating agents Escherichia coli