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Related Experiment Videos

Urate oxidase: primary structure and evolutionary implications.

X W Wu1, C C Lee, D M Muzny

  • 1Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.

Proceedings of the National Academy of Sciences of the United States of America
|December 1, 1989
PubMed
Summary
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Humans lack functional urate oxidase (uricase) due to two nonsense mutations. This loss, crucial for uric acid metabolism, likely resulted from a sudden evolutionary event, not gradual degradation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Urate oxidase (uricase) is a peroxisomal enzyme vital for uric acid breakdown in most mammals.
  • Humans and some primates lack functional uricase due to an unknown mechanism.
  • Understanding this loss is key to comprehending human metabolic differences.

Purpose of the Study:

  • To identify the molecular basis for the loss of urate oxidase (uricase) in humans.
  • To compare urate oxidase gene sequences across species to understand evolutionary divergence.

Main Methods:

  • Isolation and DNA sequencing of urate oxidase cDNA clones from pig, mouse, and baboon.
  • Sequencing of mouse and pig genomic copies of the urate oxidase gene.
  • Sequence comparison and analysis of human urate oxidase gene.

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Main Results:

  • Identified differences in polypeptide length (303-304 amino acids) due to codon events between species.
  • Confirmed a type 2 copper binding motif in urate oxidase sequences.
  • Discovered two nonsense mutations in the human urate oxidase gene, rendering it nonfunctional.
  • Sequence data supports a sudden mutational event as the cause of uricase loss in humans.

Conclusions:

  • The human urate oxidase gene is nonfunctional due to specific nonsense mutations.
  • The loss of uricase in humans is likely attributed to a sudden evolutionary event.
  • Comparative sequence analysis provides molecular evidence for the evolutionary loss of this enzyme.