Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.

@article{Nasu1978SynthesisOQ,
  title={Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.},
  author={S Nasu and Floyd Wicks and Shigeki Sakakibara and R. K. Gholson},
  journal={Biochemical and biophysical research communications},
  year={1978},
  volume={84 4},
  pages={
          928-35
        }
}
  • S. Nasu, F. Wicks, R. Gholson
  • Published 30 October 1978
  • Biology, Chemistry
  • Biochemical and biophysical research communications
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7 Citations

7 Citations

Citation Type

Citation Type

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.
Replacement of the B protein requirement of the E. coli quinolinate synthetase system by chemically-generated iminoaspartate.
  • S. Nasu, R. Gholson
  • Chemistry, Biology
    Biochemical and biophysical research communications
  • 1981
Structural basis for the catalytic activities of the multifunctional enzyme quinolinate synthase
Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product.
TLDR
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.
Peroxisomal oxidases and suggestions for the mechanism of action of insulin and other hormones.
  • G. A. Hamilton
  • Medicine
    Advances in enzymology and related areas of molecular biology
  • 1985
7 - Biosynthetic and Salvage Pathways of Pyridine Nucleotide Coenzymes

References

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Occurrence in mammalian liver of a protein which replaces the B protein of E. coli quinolinate synthetase.
Studies on the de novo biosynthesis of NAD in Escherichia coli. V. Properties of the quinolinic acid synthetase system.
Studies on the de novo biosynthesis of NAD in Escherichia coli. II. Quantitative method for isolating quinolinic acid from biological materials.
THE ENZYMATIC CONVERSION OF QUINOLINATE TO NICOTINIC ACID MONONUCLEOTIDE IN MAMMALIAN LIVER.
TLDR
The work of Nishizuka and Hayaishi clearly establishes a possible enzymatic basis for t,he conversion of tryptophan t,o niacin, but leaves unanswered several basic questions concerning this conversion.
The mode of condensation of aspartic acid and dihydroxyacetone phosphate in quinolinate synthesis in Escherichia coli.
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 ACTIVITY IN EXTRACTS OF MAMMALIAN CENTRAL NERVOUS TISSUE
Abstract— d‐Aspartate oxidase activity has been measured in water extracts of acetone powders prepared from cat forebrain, cerebellum and spinal cord, rat brain, hog brain and sheep brain stem, and…
Improved direct method for determination of keto acids by 2,4-dinitrophenylhydrazine.
Quinolinic acid metabolism; urinary excretion by the rat following tryptophan and 3-hydroxyanthranilic acid administration.