Substitution of lysine for arginine at position 199 of a hypoxanthine phosphoribosyltransferase interferes with binding of the primary substrate to the active site

Sydney P. Craig*, Pamela J. Focia, Robert J. Fletterick

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Lysine was substituted for a conserved arginine at position 199 of the schistosomal hypoxanthine phosphoribosyltransferase (HPRT). This resulted in a ≤ 35-fold increase in the K(M) for binding phosphoribosyl-pyrophosphate (PRPP). The possible functional role of R199 in tertiary structure, as well as in the binding of PRPP, is interpreted in the context of the reported three dimensional structure for the human HPRT.

Original languageEnglish (US)
Pages (from-to)1-3
Number of pages3
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1339
Issue number1
DOIs
StatePublished - Apr 25 1997

Keywords

  • Mutagenesis
  • Phosphoribosyltransferase
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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