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      The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family.

      1 , , ,
      Genomics
      Elsevier BV

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          Abstract

          A physiological role for paraoxonase (PON1) is still uncertain, but it catalyzes the hydrolysis of toxic organophosphates. Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here. Human PON1 and PON2 each have nine exons, and the exon/intron junctions occur at equivalent positions. PON1 and PON2 genes are both on chromosome 7 in human and on chromosome 6 in the mouse. Turkey and chicken, like most birds, lack paraoxonase activity and are very susceptible to organophosphates. However, they have a PON-like gene with approximately 70% identity with human PON1, PON2, and PON3. Another unexpected finding is that the deduced amino acid sequences of PON2 in human, mouse, dog, turkey, and chicken and of human PON3 are all missing the amino acid residue 105, which is lysine in human PON1. The expanded number of PON genes will have important implications for future experiments designed to discover the individual functions, catalytic properties, and physiological roles of the paraoxonases.

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          Author and article information

          Journal
          Genomics
          Genomics
          Elsevier BV
          0888-7543
          0888-7543
          May 01 1996
          : 33
          : 3
          Affiliations
          [1 ] Department of Anesthesiology, University of Michigan Medical School, R5036 Kresge II Building, Ann Arbor, Michigan, 48109-0572, USA.
          Article
          S0888754396902256
          10.1006/geno.1996.0225
          8661009
          8cc24ac6-2b81-4847-b0fd-42f4be5bd51e
          History

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