Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine.

@article{Westrop2006CysteineBI,
  title={Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine.},
  author={Gareth D Westrop and Gordon Goodall and Jeremy C Mottram and Graham H. Coombs},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 35},
  pages={
          25062-75
        }
}
Trichomonas vaginalis is an early divergent eukaryote with many unusual biochemical features. It is an anaerobic protozoan parasite of humans that is thought to rely heavily on cysteine as a major redox buffer, because it lacks glutathione. We report here that for synthesis of cysteine from sulfide, T. vaginalis relies upon cysteine synthase. The enzyme (TvCS1) can use either O-acetylserine or O-phosphoserine as substrates. The K(m) values of the enzyme for sulfide are very low (0.02 mm… CONTINUE READING