The nature of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase in extracts of wild-type Neurospora crassa: a reaction controlled by two activating substrates and three allosteric negative modifiers.

@article{Doy1968TheNO,
  title={The nature of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase in extracts of wild-type Neurospora crassa: a reaction controlled by two activating substrates and three allosteric negative modifiers.},
  author={Colin H. Doy},
  journal={Biochimica et biophysica acta},
  year={1968},
  volume={159 2},
  pages={
          352-66
        }
}
  • C. H. Doy
  • Published 4 June 1968
  • Biology
  • Biochimica et biophysica acta

The kinetics of a purified form of 3-deoxy-D-arabino heptulosonate-7-phosphate synthase (tryptophan) from Neurospora crassa.

  • K. IpC. H. Doy
  • Biology, Computer Science
    European journal of biochemistry
  • 1979
The substrates phosphoenolpyruvate and erythrose 4-phosphate and the product inorganic phosphate can protect the purified enzyme against heat denaturation, whereas the inhibitor, tryptophan, has no effect, although it binds to the enzyme in the absence of other ligands.

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe)from Escherichia coli K12. 2. Kinetic properties.

The effects of pH ON V and V/(Km for phosphoenolpyruvate) indicated that an ionizing group of pKa 8.0-8.1 is involved in the catalytic activity of the enzyme and the pKa of this group is unaffected by the binding of phosphate.

Feedback Regulation of 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthetase from a Marine Bacterium, Vibrio MB22

A marine bacterium, Vibrio MB22, has been studied to determine the pattern of feedback regulation of the first enzyme unique to the biosynthesis of the aromatic amino acids,

References

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Chromatography of 3-deoxy-D-arabinoheptulosonic acid-7-phosphate synthetase (trp) on diethylaminoethyl cellulose: a correction

The purpose of this note is to explain the nature of these artifacts and to present the elution profile of DAHP synthetase (trp), which is found in cell-free extracts prepared from cells grown in minimal medium alone and found a single peak of enzyme activity in fractions 37 to 40.

The biosynthesis of aromatic compounds from D-glucose.

Genetic and Biochemical Analysis of the Isoenzymes Concerned in the First Reaction of Aromatic Biosynthesis in Escherichia coli

Mutant strains of Escherichia coli K-12 were isolated possessing mutations which affected the tyrosine-inhibitable 3-deoxy-d-arabinoheptulosonic acid-7-phosphate (DAHP) synthetase, the

Genetic control of the structure and activity of an enzyme aggregate in the tryptophan pathway of Neurospora crassa.

To define the role of the two genetic loci in controlling the structure and activity of the enzyme aggregate, a detailed biochemical and genetic analysis of a series of tryp-l andtryp-2 mutants is carried out.