The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.

@article{Nasu1982TheME,
  title={The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.},
  author={S Nasu and Floyd Wicks and R. K. Gholson},
  journal={Biochimica et biophysica acta},
  year={1982},
  volume={704 2},
  pages={
          240-52
        }
}
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.
Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase.
TLDR
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.
Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation.
D-aspartate oxidase (DDO, EC 1.4.3.1) catalyzes dehydrogenation of D-aspartate to iminoaspartate and the subsequent re-oxidation of reduced FAD with O2 to produce hydrogen peroxide. In the mammalian
Crystal structure of archaeal highly thermostable L‐aspartate dehydrogenase/NAD/citrate ternary complex
TLDR
This is the first detailed description of substrate and coenzyme binding to l‐aspDH and of the molecular basis of the high thermostability of a hyperthermophilic l‐aspartate dehydrogenase.
Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence analysis of the bifunctional nadR regulator and the nadA-pnuC operon
TLDR
A hypothetical model in which NadR interacts with PnuC at low internal NAD levels, permitting transport of NMN intact into the cell is suggested, suggesting that NadR is indeed bifunctional.
Crystallization and preliminary crystallographic analysis of D-aspartate oxidase from porcine kidney.
TLDR
D-Aspartate oxidase from porcine kidney was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as a precipitant and molecular-replacement trials using the structure of human D-amino-acid oxidase as a search model provided a satisfactory solution.
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References

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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.
TLDR
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
TLDR
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.
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