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

@article{Nasu1982LAspartateOA,
  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},
  year={1982},
  volume={257 2},
  pages={
          626-32
        }
}
L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.
TLDR
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.
TLDR
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.
TLDR
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
TLDR
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.
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