L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.

  title={L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.},
  author={S Nasu and Floyd Wicks and R. K. Gholson},
  journal={The Journal of biological chemistry},
  volume={257 2},
L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.
Modification of a previously published procedure allowed overexpression of the holoenzyme in an unproteolysed form and biochemical characterization of the flavoprotein L-aspartate oxidase from Escherichia coli is reported.
Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects.
NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate, according to previous kinetic and structural data.
L-aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate: fumarate oxidoreductase activity.
Evidence is presented which suggests that in vitro fumarate can be a valuable alternative to oxygen as a substrate for L-aspartate oxidase, and Steady-state kinetics for the oxidase and thefumarate reductase activity of L- aspartate oxidation were obtained.
Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria
It is shown that it is possible to recognize different groups of these enzymes and those containing the quinone cofactor are clearly differentiated, and most of the proteins described as antimicrobial because of their capacity to generate hydrogen peroxide belong to the group of LodA-like proteins.


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.
D-aspartate oxidase of kidney.
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.
Pyridine nucleotide metabolism in Escherichia coli. II. Niacin starvation.
The changes in the distribution of the pyridine nucleotides suggest that DPN is turning over during niacin starvation and that the normally observed breakdown of TPN to DPN during exponential growth is inhibited.
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
The condensation step in diaminopimelate synthesis.
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