Tryptophan hydroxylase. The role of oxygen, iron, and sulfhydryl groups as determinants of stability and catalytic activity.

@article{Kuhn1980TryptophanHT,
  title={Tryptophan hydroxylase. The role of oxygen, iron, and sulfhydryl groups as determinants of stability and catalytic activity.},
  author={Donald M Kuhn and Barbara Ruskin and Walter Lovenberg},
  journal={The Journal of biological chemistry},
  year={1980},
  volume={255 9},
  pages={4137-43}
}
Tryptophan hydroxylase (EC 1.14.16.4) from rat mid-brain is inactivated upon exposure to oxygen. The degree of inactivation is dependent both on the temperature and partial pressure of oxygen to which the enzyme is exposed. Furthermore, molecular oxygen, and not an oxygen or hydroxyl radical, is responsible for the inactivation. Sulfhydryl compounds and reductants partially protect the hydroxylase from inactivation by oxygen. Enzyme inhibited by oxygen can be reconstituted by anaerobic… CONTINUE READING
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