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L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase.
In Escherichia coli, quinolinic acid, a precursor of NAD+, is synthesized from L-aspartate and dihydroxyacetone phosphate, which requires two enzymes, a FAD-containing "B protein" and an "A protein" that behaves as an L- aspartate oxidase, which displays some unusual properties.
The effect of pyrazines on the metabolism of tryptophan and nicotinamide adenine dinucleotide in the rat. Evidence of the formation of a potent inhibitor of aminocarboxy-muconate-semialdehyde
Results suggest that the glutarate pathway of L-tryptophan was strongly inhibited by the inhibitor produced after the administration of pyrazinoic acid and pyrazinamide, which exhibited a significant inhibition of the nuclear enzyme poly(ADP-ribose) synthetase in rat liver.
Replacement of the B protein requirement of the E. coli quinolinate synthetase system by chemically-generated iminoaspartate.
  • S. Nasu, R. Gholson
  • Biology, Medicine
    Biochemical and biophysical research…
  • 30 July 1981
This finding supports the concept that the B protein (L- aspartate oxidase) functions to form iminoaspartate which is condensed with dihydroxyacetone phosphate by the A protein to form quinolinate.
Identification of the 3' 5' - cyclic AMP phosphodiesterase inhibitor in potato: feed-back control by inorganic phosphate.
It is found that the partially purified inhibitor yielded an elution pattern and a phosphodiesterase inhibition identical with those of inorganic phosphate in Sephadex G-25 column chromatography, and finding that the Rf value for this inhibitor agreed with that for in Organic phosphate on paper chromatographic analysis, is able to identify this inhibitor as in organic phosphate.
Ca2+/protein modulator-dependent and -independent cyclic GMP phosphodiesterase from hog heart.
The Ca2+/protein modulator-dependent enzyme proved relatively stable at 48 degrees C for 1 h, but the independent form lost its activity under the same conditions, whereas the plots for the independent enzyme were anomalous, showing both high and low K m values for cGMP.
The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase.
In Escherichia coli quinolinic acid, a precursor of NAD+, is synthesized from L-aspartate and dihydroxyacetone phosphate by two enzymes, an FAD-containing 'B protein' and 'A protein'. An enzyme which
Synthesis of quinolinate from D-aspartate in the mammalian liver-Escherichia coli quinolinate synthetase system.
Observations suggest that liver Bprotein is D-aspartate oxidase and E. coli B protein is L-as Partic acid oxidase, which is a substrate for quinolinic acid synthesis in a system composed of the B protein replacing activity of mammalian liver andE.
Inhibition of adenosine 3',5'-monophosphate phosphodiesterase by nicotinamide and its homologues in vitro.
Inhibition of cAMP phosphodiesterase from rat liver by nicotinamide and its homologues was studied and a comparison of the inhibitory curves of theophylline, papaverine, and ethylnicotinate on enzyme activity showed them to be approximately coincident.
Effect of L-leucine-supplemented diet on the nicotinamide adenine dinucleotide content of rat liver.
The findings strongly suggest that decrease in the liver NAD content by excess dietary leucine is mainly due to competitive inhibition by L-leucine of intestinal absorption of L-tryptophan.
Separation of multiple forms of cyclic nucleotide phosphodiesterase from hog heart.
  • S. Nasu
  • Chemistry, Medicine
    Bulletin of the Osaka Medical School
  • 1 October 1976