Cofactors

Iron-sulfur.

Reaction Mechanism

There are no Reaction Mechanism for this Enzyme

Reaction Parameters

• Kinetic Parameters

  Organism	KM Value [mM]	Substrate	Comment
  Bacillus subtilis	0.36	dihydroxyacetone phosphate	25°C

• Temperature

  There are no reaction parameters information for this Enzyme.

• pH

  There are no reaction parameters information for this Enzyme.

Associated Proteins

Citations

• Over-expressing NadA quinolinate synthase in Escherichia coli enhances the bioelectrochemistry in microbial fuel cells.
• Quinolinate Synthase: An Example of the Roles of the Second and Outer Coordination Spheres in Enzyme Catalysis.
• Metabolic engineering of Escherichia coli for quinolinic acid production by assembling L-aspartate oxidase and quinolinate synthase as an enzyme complex.
• Design of specific inhibitors of quinolinate synthase based on [4Fe-4S] cluster coordination.
• The cloning and characterization of hypersensitive to salt stress mutant, affected in quinolinate synthase, highlights the involvement of NAD in stress-induced accumulation of ABA and proline.
• An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.
• Structure of Quinolinate Synthase from Pyrococcus horikoshii in the Presence of Its Product, Quinolinic Acid.
• Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product.
• Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.
• Dual activity of quinolinate synthase: triose phosphate isomerase and dehydration activities play together to form quinolinate.
• Active-site models for complexes of quinolinate synthase with substrates and intermediates.