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.

@article{Griffith1975StudiesOT,
  title={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.},
  author={Gary R. Griffith and Jennifer Chandler and R. K. Gholson},
  journal={European journal of biochemistry},
  year={1975},
  volume={54 1},
  pages={
          239-45
        }
}
Quinolinic acid (pyridine 2,3-dicarboxylic acid) which is an immediate precursor of the pyridine nucleotides, is synthesised from L-asparate and dihydroxyacetone phosphate in Escherichia coli. Extracts from certain nadB mutants complement the extracts prepared from all nadA mutants for the enzymic synthesis of quinolinate. Using the complementation assay, the quinolinate synthetase B protein has been purified more than 300-fold. The quinolinate synthetase B protein exists in all nadA and nadC… 
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Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB.
TLDR
Both gene products seem to be equally rate-limiting in quinolinate synthesis, according to sequence analysis and promoter regions and ribosomal binding sites were assigned by comparison to consensus sequences.
Quinolinate synthetase, an iron–sulfur enzyme in NAD biosynthesis
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
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.
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.
Covalent Flavinylation of L-Aspartate Oxidase from Escherichia coli Using N6-(6-Carboxyhexyl)-FAD Succinimidoester
TLDR
Comparison of some properties of the flavinylated and native enzymes suggests that, although the flavin is covalently bound to the former in the region predicted from molecular modeling studies, the microenvironment around the isoallossazine is different in the two forms.
Characterization of l‐aspartate oxidase and quinolinate synthase from Bacillus subtilis
TLDR
It was shown that the interaction between NadA and NadB is not species‐specific between B. subtilis and Escherichia coli, and a new noncanonical binding motif that, on the basis of sequence alignment studies, may be common to other quinolinate synthases from different organisms.
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.
fusB is an allele of nadD, encoding nicotinate mononucleotide adenylyltransferase in Escherichia coli.
TLDR
This work shows that the fusB mutation is a frameshift mutation in the nadD gene that encodes nicotinate mononucleotide adenylyltransferase, and that a small decrease in NAD+ levels affects ability to grow on minimal medium at 42 degrees C, while a large decrease leads to a more pleiotropic phenotype.
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References

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TLDR
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TLDR
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TLDR
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