Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels.

@article{Stipanuk2002EnzymesAM,
  title={Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels.},
  author={Martha H. Stipanuk and Monica P Londono and Jeong-In Lee and Mindy Hu and Anthony F. Yu},
  journal={The Journal of nutrition},
  year={2002},
  volume={132 11},
  pages={3369-78}
}
In liver, cysteine dioxygenase (CDO), cysteinesulfinate decarboxylase (CSD), and gamma-glutamylcysteine synthetase (GCS) play important regulatory roles in the metabolism of cysteine to sulfate, taurine and glutathione. Because glutathione is released by the liver and degraded by peripheral tissues that express gamma-glutamyl transpeptidase, some peripheral tissues may be exposed to relatively high concentrations of cysteine. Rats were fed diets that contained low, moderate or high… CONTINUE READING

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