CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding.

@article{Sherbet2003CYP17ME,
  title={CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding.},
  author={Daniel P Sherbet and Dov Tiosano and Kerri M Kwist and Z{\`e}ev Hochberg and Richard J Auchus},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 49},
  pages={48563-9}
}
Cytochrome p450c17 (CYP17) converts the C21 steroids pregnenolone and progesterone to the C19 androgen precursors dehydroepiandrosterone (DHEA) and androstenedione, respectively, via sequential 17alpha-hydroxylase and 17,20-lyase reactions. Disabling mutations in CYP17 cause combined 17alpha-hydroxylase/17,20-lyase deficiency, but rare missense mutations cause isolated loss of 17,20-lyase activity by disrupting interactions of redox partner proteins with CYP17. We studied an adolescent male… CONTINUE READING

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