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Literature summary extracted from

  • Reichmann, D.; Coute, Y.; Ollagnier de Choudens, S.
    Dual activity of quinolinate synthase: triose phosphate isomerase and dehydration activities play together to form quinolinate (2015), Biochemistry, 54, 6443-6446.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.72 drug development te enzyme is required for the biosynthesis of NAD. Besides the de novo pathway for NAD synthesis, a salvage pathway exists in some organisms allowing NAD to be recycled from nicotinic acid and nicotinamide. Some pathogens such as Mycobacterium leprae and Helicobacter pylori lack this salvage pathway. The different pathways for quinolinate biosynthesis in most prokaryotes and eukaryotes, combined with the fact that the salvage pathway is absent in some pathogenic microorganisms, make enzyme NadA an ideal target in the search for specific antibacterial drugs Escherichia coli K-12
2.5.1.72 drug development te enzyme is required for the biosynthesis of NAD. Besides the de novo pathway for NAD synthesis, a salvage pathway exists in some organisms allowing NAD to be recycled from nicotinic acid and nicotinamide. Some pathogens such as Mycobacterium leprae and Helicobacter pylori lack this salvage pathway. The different pathways for quinolinate biosynthesis in most prokaryotes and eukaryotes, combined with the fact that the salvage pathway is absent in some pathogenic microorganisms, make enzyme NadA an ideal target in the search for specific antibacterial drugs Thermotoga maritima

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.72 Phosphoglycolic acid significantly inhibits the enzyme's triose phosphate isomerase activity at 1 mM Escherichia coli K-12
2.5.1.72 Phosphoglycolic acid significantly inhibits the enzyme's triose phosphate isomerase activity at 1 mM Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.72 Fe2+ an [4Fe-4S] cluster-containing enzyme Escherichia coli K-12
2.5.1.72 Fe2+ an [4Fe-4S] cluster-containing enzyme Thermotoga maritima
2.5.1.72 [4Fe-4S] cluster an [4Fe-4S] cluster-containing enzyme. The Fe/S cluster of NadA (both Fe4S4 and Fe2S2) might play a significant structural role in NadA that could affect the triose phosphate isomerase activity Escherichia coli K-12
2.5.1.72 [4Fe-4S] cluster an [4Fe-4S] cluster-containing enzyme. The Fe/S cluster of NadA (both Fe4S4 and Fe2S2) might play a significant structural role in NadA that could affect the triose phosphate isomerase activity Thermotoga maritima

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 Escherichia coli K-12
-
 pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
 ?
2.5.1.72 glycerone phosphate + iminosuccinate Thermotoga maritima
-
 pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.72 Escherichia coli K-12 P11458 gene nadA
-
2.5.1.72 Thermotoga maritima Q9X1X7 gene nadA
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.72 glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate reaction mechanism with an early release of phosphate from dihydroxyacetone phosphate, that only, not glycerol 3-phosphate, can condense with iminoaspartate to form quinolinate. The NadA three-dimensional structure shows that there is no room in the active site to accommodate a condensation product on which the phosphate group from dihydroxyacetone phosphate is still present, overview. The enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner Escherichia coli K-12
a
2.5.1.72 glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate reaction mechanism with an early release of phosphate from dihydroxyacetone phosphate, that only, not glycerol 3-phosphate, can condense with iminoaspartate to form quinolinate. The NadA three-dimensional structure shows that there is no room in the active site to accommodate a condensation product on which the phosphate group from dihydroxyacetone phosphate is still present, overview. The enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner Thermotoga maritima
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.72 glycerone phosphate + iminosuccinate
-
 Escherichia coli K-12 pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
 ?
2.5.1.72 glycerone phosphate + iminosuccinate
-
 Thermotoga maritima pyridine-2,3-dicarboxylate + 2 H2O + phosphate
-
 ?
2.5.1.72 additional information the enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner. Only dihydroxyacetone phosphate can then condense with iminoaspartate to form quinolinate. If glycerol 3-phosphate is not converted to dihydroxyacetone phosphate no quinolinate can be produced. The enzyme as triose phosphate isomerase is more efficient in the direction of dihydroxyacetone phosphate production Escherichia coli K-12 ?
-
 ?
2.5.1.72 additional information the enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner. Only dihydroxyacetone phosphate can then condense with iminoaspartate to form quinolinate. If glycerol 3-phosphate is not converted to dihydroxyacetone phosphate no quinolinate can be produced. The enzyme as triose phosphate isomerase is more efficient in the direction of dihydroxyacetone phosphate production Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.72 NadA
-
 Escherichia coli K-12
2.5.1.72 NadA
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.72 37
-
 assay at Escherichia coli K-12
2.5.1.72 37
-
 assay at Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.72 7.5
-
 assay at Escherichia coli K-12
2.5.1.72 7.5
-
 assay at Thermotoga maritima

General Information

EC Number General Information Comment Organism
2.5.1.72 physiological function quinolinate synthase is an [4Fe-4S] cluster-containing dehydrating enzyme involved in synthesis of quinolinic acid, the universal precursor of the essential coenzyme nicotinamide adenine dinucleotide Escherichia coli K-12
2.5.1.72 physiological function quinolinate synthase is an [4Fe-4S] cluster-containing dehydrating enzyme involved in synthesis of quinolinic acid, the universal precursor of the essential coenzyme nicotinamide adenine dinucleotide Thermotoga maritima