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Literature summary for 2.5.1.72 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
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Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline inhibits reactivation of O2-inactivated enzyme Escherichia coli
2,2'-dipyridyl inhibits reactivation of O2-inactivated enzyme Escherichia coli
H2O2 1 mM, inactivation Escherichia coli
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
paraquat inactivation Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
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

Cofactor Comment Organism Structure
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