Substitution of lysine for arginine at position 199 of a hypoxanthine phosphoribosyltransferase interferes with binding of the primary substrate to the active site
被引:7
作者:
Craig, SP
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机构:UNIV PUERTO RICO,DEPT BIOCHEM,SAN JUAN,PR 00936
Craig, SP
Focia, PJ
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机构:UNIV PUERTO RICO,DEPT BIOCHEM,SAN JUAN,PR 00936
Focia, PJ
Fletterick, RJ
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机构:UNIV PUERTO RICO,DEPT BIOCHEM,SAN JUAN,PR 00936
Fletterick, RJ
机构:
[1] UNIV PUERTO RICO,DEPT BIOCHEM,SAN JUAN,PR 00936
[2] UNIV CALIF SAN FRANCISCO,DEPT PHARMACEUT CHEM,SAN FRANCISCO,CA 94143
来源:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
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1997年
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1339卷
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01期
Lysine was substituted for a conserved arginine at position 199 of the schistosomal hypoxanthine phosphoribosyltransferase (HPRT). This resulted in a greater than or equal to 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.