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

Jihad Obeid, Perrin C. White

Research output: Contribution to journalArticle

103 Citations (Scopus)

Abstract

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
Volume188
Issue number1
DOIs
StatePublished - Oct 15 1992

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11-beta-Hydroxysteroid Dehydrogenases
Mutagenesis
CHO Cells
Corticosterone
Site-Directed Mutagenesis
Rats
Oxidoreductases
Complementary DNA
Amino Acids
Mutation
Enzymes
11-dehydrocorticosterone

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. / Obeid, Jihad; White, Perrin C.

In: Biochemical and Biophysical Research Communications, Vol. 188, No. 1, 15.10.1992, p. 222-227.

Research output: Contribution to journalArticle

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