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={James Nigel Burnell and Frederick Robert Whatley},
  journal={Biochimica et biophysica acta},
  year={1977},
  volume={481 1},
  pages={
          246-65
        }
}
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… 
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Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of cysteinyl-and methionyl-tRNA synthetase.
Cysteinyl- and methionyl-tRNA synthetases (EC 6.11.-) were purified 1200- and 1000-fold, respectively, from sonic extracts of Paracoccus denitrificans strain 8944, and kinetics, substrate specificity…
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  • Chemistry, Medicine
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  • 1981
TLDR
It seems that selenium-containing amino acids are excluded from proteins by a mechanism(s) other than substrate discrimination at the amino acid activation stage of protein synthesis.
Purification and physicochemical characterization of O-acetyl-l-serine sulfhydrylase from Chlamydomonas reinhardtii
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L -Cyteine and l -Methionine are effective inhibitors of the OASSase activity, which is also inhibited by hydroxylamine and p-hydroxymercuribenzoate (pHMB).
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Toxicity assays performed with the various mutant proteins obtained by site-directed mutagenesis established that only catalytically active forms of beta-cystathionase were were cytotoxic for tissue culture cells.
Purification and characterization of cystathionine γ‐lyase from Lactobacillus fermentum DT41
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Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase
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This study found that various strains of L. casei grew in a chemically defined medium containing sulfide as the sole sulfur source, indicating the presence of a serine O-acetyltransferase and demonstrated that the gene annotated as metA in fact encodes the SAT function and should be annotation as cysE.
Role of d-Cysteine Desulfhydrase in the Adaptation of Escherichia coli to d-Cysteine*
TLDR
In agreement with a role of the desulfhydrase in sulfur metabolism, yedO expression was induced under conditions of sulfate limitation and growth protection against d-cysteine in minimal medium was conferred by the simultaneous addition of isoleucines, leucine, and valine.
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