On the metabolic role of thymidine 2′‐hydroxylase (thymidine, 2‐oxoglutarate: Oxygen oxidoreductase, EC 1.14.11.3) in Neurospora crassa

@article{Bankel1976OnTM,
  title={On the metabolic role of thymidine 2′‐hydroxylase (thymidine, 2‐oxoglutarate: Oxygen oxidoreductase, EC 1.14.11.3) in Neurospora crassa},
  author={Lorenz Bankel and G{\"o}ran Lindstedt and Sven Torvald Lindstedt},
  journal={FEBS Letters},
  year={1976},
  volume={71}
}
3 Citations
Optimization of Culture Conditions for the Production of Pyrimidine Nucleotide N-Ribosidase from Pseudomonas oleovorans
TLDR
The pyrimidine nucleotide N-ribosidase of P. oleovorans ATCC 8062 was not induced by UMP and its derivatives, and was constitutive enzyme.

References

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Thymidine 2'-hydroxylation in Neurospora crassa.
A kinetic study of thymine 7-hydroxylase from neurospora crassa.
TLDR
The steady-state kinetics of thymine 7-hydroxylase (thymine, 2-oxoglutarate dioxygenase, EC 1.11.6) has been investigated and initial velocity plots were found to be linear and intersecting, consistent with an ordered sequential kinetic mechanism.
Mutants Affecting Thymidine Metabolism in Neurospora crassa
TLDR
Three mutants were isolated in which different steps are blocked in the pathway that converts the pyrimidine ring of thymidine to an RNA precursor, and three other classes of mutations are proposed to be affecting, respectively, regulation of theThymidine degradative pathway, transport of pyridine free bases, and transport ofpyrimidine nucleosides.
Metabolism of pyrimidine deoxyribonucleosides in Neurospora crassa
The experiments in this report involve the following series of reactions which were previously demonstrated with purified enzyme preparations from Neurospora crassa: thymidine a yields thymine
The oxidation in liver of l-tyrosine to acetoacetate through p-hydroxyphenylpyruvate and homogentisic acid.
TLDR
A more active L-tyrosine oxidation system than any hitherto used, freed from other reactions occurring in crude liver homogenates, was needed to investigate these discrepancies.
Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase.
  • R. RhoadsS. Udenfriend
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1968
TLDR
With these preparations, it has now been possible to show a substrate-dependent and stoichiometric decarboxylation of a--ketoglutarate coupled to the hydroxylations of peptidyl proline residues.
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