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Literature summary 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

EC Number Protein Variants Comment Organism
2.5.1.72 E198Q site-directed mutagenesis, inactive mutant Pyrococcus horikoshii
2.5.1.72 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
2.5.1.72 Y109F site-directed mutagenesis, inactive mutant Pyrococcus horikoshii
2.5.1.72 Y23F site-directed mutagenesis, inactive mutant Pyrococcus horikoshii

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.72 Pyrococcus horikoshii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.72 glycerone phosphate + iminosuccinate
-
 Pyrococcus horikoshii pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
 ?
2.5.1.72 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

EC Number Synonyms Comment Organism
2.5.1.72 NadA
-
 Pyrococcus horikoshii

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.72 [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

EC Number General Information Comment Organism
2.5.1.72 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
2.5.1.72 physiological function quinolinate synthase is involved in synthesis of quinolinic acid, the universal precursor of the essential coenzyme nicotinamide adenine dinucleotide Pyrococcus horikoshii