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 language||English (US)|
|Number of pages||3|
|Journal||Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology|
|State||Published - Apr 25 1997|
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology