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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.

Keywords

Codon Methionine Guanine Amino Acid Substitution Isoelectric Point 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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