Occurrence in mammalian liver of a protein which replaces the B protein of E. coli quinolinate synthetase.

@article{Sakakibara1977OccurrenceIM,
  title={Occurrence in mammalian liver of a protein which replaces the B protein of E. coli quinolinate synthetase.},
  author={Shigeki Sakakibara and Floyd Wicks and R. K. Gholson},
  journal={Biochemical and biophysical research communications},
  year={1977},
  volume={76 1},
  pages={
          158-66
        }
}
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7 Citations

7 Citations

Citation Type

Citation Type

Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
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.
Presence of D-aspartate oxidase in rat liver and mouse tissues.
Preliminary crystallographic studies on quinolinate phosphoribosyltransferase.
7 - Biosynthetic and Salvage Pathways of Pyridine Nucleotide Coenzymes

References

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TLDR
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TLDR
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TLDR
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