Clinical and biochemical manifestations and molecular characterization of the mutation HPRT Jerusalem

E. Zoref-Shani, Y. Bromberg, J. Hirsch, S. Feinstein, Y. Frishberg, O. Sperling

Research output: Contribution to journalArticlepeer-review

Abstract

A novel point mutation (I137T) was identified in the hypoxanthine-guanine phosphoribosyltransferase (HPRT) encoding gene, in a patient with partial deficiency of the enzyme. The mutation, ATT to ACT (substitution of isoleucine to threonine), occurred at codon 137, which is within the region encoding the binding site for 5-phosphoribosyl-1-pyrophosphate (PRPP). The mutation caused decreased affinity for PRPP, manifested clinically as a Lesch-Nyhan variant (excessive purine production and delayed acquisition of language skills). The partial HPRT deficiency could be detected only by measuring HPRT activity in intact fibroblasts (uptake of hypoxanthine into nucleotides).

Original languageEnglish
Pages (from-to)1165-1168
Number of pages4
JournalNucleosides, Nucleotides and Nucleic Acids
Volume23
Issue number8-9
DOIs
StatePublished - 2004

Keywords

  • 5-Phosphoribosyl-1-pyrophosphate
  • Hypoxanthine-guanine phosphoribosyltransferase
  • Lesch-Nyhan variant

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