Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase

Jihad Obeid, Perrin C. White

Research output: Contribution to journalArticlepeer-review

105 Scopus citations


Tyr-179 and Lys-183 are likely to be functionally important residues in 11β-hydroxysteroid dehydrogenase, as thease amino acids are absolutely conserved in all members of the "short chain dehydrogenase" family. We modified these residues by site-directed mutagenesis of rat cDNA and transfected these constructs into CHO cells. A highly but not absolutely conserved residue, Asp-110, was also studied. Mutation of Tyr-179 to Phe or Ser completely abolished enzymatic activity (interconversion of corticosterone and 11-dehydrocorticosterone), as did Lys-183→Arg. Asp-110→Asn affected activity only mildly. Tyr-179 and Lys-183 may be directly involved in the catalytic function of this class of enzymes.

Original languageEnglish (US)
Pages (from-to)222-227
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Oct 15 1992

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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