Introduction of a metal-dependent regulatory switch into an enzyme.

D. R. Corey, P. G. Schultz

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

A cysteine has been introduced into the hydrophobic binding pocket of staphylococcal nuclease via oligonucleotide-directed mutagenesis. The L89C mutation does not significantly alter the catalytic activity or specificity of the nuclease yet provides a metal-dependent switch for regulating enzymatic activity. The L89C mutant can be inactivated by addition of mercuric or cupric salts and subsequently reactivated by addition of chelating agents. This work may provide a general strategy for regulating the catalytic activity of other enzymes or the binding affinity of proteins to DNA or other proteins.

Original languageEnglish (US)
Pages (from-to)3666-3669
Number of pages4
JournalThe Journal of biological chemistry
Volume264
Issue number7
StatePublished - Mar 5 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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