Replacement of the B protein requirement of the E. coli quinolinate synthetase system by chemically-generated iminoaspartate.

  title={Replacement of the B protein requirement of the E. coli quinolinate synthetase system by chemically-generated iminoaspartate.},
  author={S Nasu and R. K. Gholson},
  journal={Biochemical and biophysical research communications},
  volume={101 2},
  • S. Nasu, R. Gholson
  • Published 30 July 1981
  • Chemistry, Biology
  • Biochemical and biophysical research communications
Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase.
To study the mechanism of action, the specificity of the enzyme and the interaction with l-aspartate oxidase, the other component of the so-called "quinolinate synthetase complex," the cloning, the overexpression, and the purification to homogeneity of Escherichia coli quinolinate Synthetase were undertaken.
Structure of Quinolinate Synthase from Pyrococcus horikoshii in the Presence of Its Product, Quinolinic Acid.
The structure of NadA is presented and it is found that N1 and the C7 carboxylate group of QA ligate to Fea in a bidentate fashion, which is confirmed by Hyperfine Sublevel Correlation (HYSCORE) spectroscopy.
Active-site models for complexes of quinolinate synthase with substrates and intermediates.
The structure of QS from Pyrococcus furiosus has been determined at 2.8 Å resolution and is a homodimer consisting of three domains per protomer, suggesting that the domains are the result of gene triplication.
An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.
A structure of NadA from Pyrococcus horikoshii (PhNadA) is presented and it is shown that a carboxylate group of the molecule is ligated to Fea of the iron-sulfur cluster, occupying the site to which DHAP has been proposed to bind during catalysis.
Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product.
The crystal structures of complexes between the Thermotoga maritima (Tm) NadA K219R/Y107F variant and the first intermediate (W) resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate are reported, shedding significant light on the mechanism of the reaction catalyzed by NadA.
Incorporation of 13 C glucose into nicotinamide in E. coli and in S. cerevisiae
The mode of incorporation into nicotinamide of label from 13C-labeled samples of D-glucose, in Escherichia coli and Saccharomyces cerevisiae, was determined by means of 13C NMR spectroscopy. The
Etude structurale et fonctionnelle de la quinolinate synthase : une protéine fer-soufre cible d'agents antibactériens
La Quinolinate synthase (NadA) catalyse la condensation de l’iminoaspartate et de la dihydroxyacetone phosphate aboutissant a la formation d’acide quinolinique, un intermediaire central dans la
The Pennsylvania State University
This work focuses on electronic transport and defect structure in multiple novel dielectric systems used for back end of line (BEOL) applications. BEOL dielectrics with low dielectric constants, so


Evidence for an intermediate in quinolinate biosynthesis in Escherichia coli
Results of these experiments indicate that the nadB gene product forms an unstable compound from aspartate in the presence of flavine adenine dinucleotide, and that this compound is then condensed with dihydroxyacetone phosphate to form quinolinate in a reaction catalyzed by the n adA gene product.
Modification of aspartate before its condensation with dihydroxyacetone phosphate during quinolinic acid formation in Escherichia coli
A crude enzyme preparation from a nadA mutant of Escherichia coli was used to catalyze the conversion of [14C]aspartic acid into a precursor of quinolinic acid, a key intermediate in the biosynthesis
Cross-Feeding of Escherichia coli Mutants Defective in the Biosynthesis of Nicotinamide Adenine Dinucleotide
Mutants of Escherichia coli defective in the biosynthesis of nicotinamide adenine dinucleotide are able to grow in a Casamino Acids medium lacking NAD and its immediate precursors, nicotinic acid and Nicotinamide, providing a means of isolating the intermediate, prequinolinic acid, as well as a biological assay for the compound.
Studies on the de novo biosynthesis of NAD in Escherichia coli. The separation of the nadB gene product from the nadA gene product and its purification.
The facile separation of the wild-type quinolinate synthetase A and B proteins out of a nadC mutant suggests that quinolinic acid does not exists as a tightly bound complex.
Detection of precursors of quinolinic acid in Escherichia coli.
A technique is described which allows the detection of precursors of quinolinic acid produced by Escherichia coli, independent of a bioassay. This is based on a double autoradiogram utilizing