Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase.

@article{Burnell1977SulphurMI,
  title={Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase.},
  author={J. Burnell and F. Whatley},
  journal={Biochimica et biophysica acta},
  year={1977},
  volume={481 1},
  pages={
          246-65
        }
}
  • J. Burnell, F. Whatley
  • Published 1977
  • Biology, Medicine
  • Biochimica et biophysica acta
    • 1. Serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase were purified from Paracoccus denitrificans strain 8944. 2. Serin transacetylase was purified 150-fold. The enzyme has a pH optimum between 7.5 and 8.0, is specific for L-serine and is inhibited by sulphydryl-group reagents. The apparent Km values for serine and acetyl-CoA are 4.0 - 10(-4) and 1.0 - 10(-4) M, respectively. Serine transacetylase is strongly inhibited by cysteine. 3. O-Acetylserine sulphydrylase was… CONTINUE READING
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