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Literature summary for 2.5.1.72 extracted from

  • Esakova, O.A.; Silakov, A.; Grove, T.L.; Saunders, A.H.; McLaughlin, M.I.; Yennawar, N.H.; Booker, S.J.
    Structure of quinolinate synthase from Pyrococcus horikoshii in the presence of its product, quinolinic acid (2016), J. Am. Chem. Soc., 138, 7224-7227.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E198Q site-directed mutagenesis, inactive mutant Pyrococcus horikoshii
additional information three strictly conserved amino acids, Glu198, Tyr109, and Tyr23, are in close proximity to the bound product. Substitution of these amino acids with Gln, Phe, and Phe, respectively, leads to complete loss of activity Pyrococcus horikoshii
Y109F site-directed mutagenesis, inactive mutant Pyrococcus horikoshii
Y23F site-directed mutagenesis, inactive mutant Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ an [4Fe-4S] cluster-containing enzyme Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycerone phosphate + iminosuccinate Pyrococcus horikoshii
-
pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycerone phosphate + iminosuccinate
-
Pyrococcus horikoshii pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
?
glycerone phosphate + iminosuccinate condensation of dihydroxyacetone phosphate (DHAP) and aspartate-enamine by the action of quinolinate synthase, NadA Pyrococcus horikoshii pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
?

Synonyms

Synonyms Comment Organism
NadA
-
Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center NadA contains a [4Fe-4S] cluster cofactor with a unique, non-cysteinyl-ligated, iron ion (Fea), which binds the hydroxyl group of a postulated intermediate in the last step of the reaction to facilitate a dehydration. N1 and the C7 carboxylate group of quinolinate ligate to Fea in a bidentate fashion placing the C5 hydroxyl group of the postulated final intermediate distal to Fea and virtually incapable of coordinating to it Pyrococcus horikoshii

General Information

General Information Comment Organism
additional information three strictly conserved amino acids, Glu198, Tyr109, and Tyr23, are in close proximity to the bound product. Substitution of these amino acids with Gln, Phe, and Phe, respectively, leads to complete loss of activity Pyrococcus horikoshii
physiological function quinolinate synthase is involved in synthesis of quinolinic acid, the universal precursor of the essential coenzyme nicotinamide adenine dinucleotide Pyrococcus horikoshii