Human Genetics

, Volume 79, Issue 1, pp 39–43 | Cite as

Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRTAnn Arbor)

  • Shin Fujimori
  • Yuji Hidaka
  • Beverly L. Davidson
  • Thomas D. Palella
  • William N. Kelley
Original Investigations

Summary

HPRTAnn Arbor is a variant of hypoxanthine (guanine) phosphoribosyl-transferase (HPRT: EC 2.4.2.8), which was identified in two brothers with hyperuricemia and nephrolithiasis. In previous studies, this mutant enzyme was characterized by an increased Km for both substrates, a normal Vmax, a decreased intracellular concentration of enzyme protein, a normal subunit molecular weight and an acidic isoelectric point under native isoelectric focusing conditions. We have cloned a full-length cDNA for HPRTAnn Arbor and determined its complete nucleotide sequence. A single nucleotide change (T→G) at nucleotide position 396 has been identified. This transversion predicts an amino acid substitution from isoleucine (ATT) to methionine (ATG) in codon 132, which is located within the putative 5′-phosphoribosyl-1-pyrophosphate (PRPP)-binding site of HPRT.

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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • Shin Fujimori
    • 1
  • Yuji Hidaka
    • 1
  • Beverly L. Davidson
    • 2
  • Thomas D. Palella
    • 1
  • William N. Kelley
    • 1
    • 2
  1. 1.Department of Internal MedicineUniversity of MichiganAnn ArborUSA
  2. 2.Department of Biological ChemistryUniversity of MichiganAnn ArborUSA

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