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Enzyme function and polymorphism: a test in two Anolis lizard species.

E Zouros, P E Hertz

    Biochemical Genetics
    |February 1, 1984
    PubMed
    Summary
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    Anolis gundlachi lizards show higher enzyme heterozygosity than Anolis roquet lizards. This difference is linked to multiple-substrate enzymes, not regulatory roles, in enzyme variability.

    Area of Science:

    • * Evolutionary biology
    • * Molecular ecology
    • * Herpetology

    Background:

    • * Enzyme variability in species is influenced by factors like enzyme function and thermal regulation.
    • * Anolis gundlachi lizards are ectothermic and experience a coarse-grained thermal environment.
    • * Anolis roquet lizards behaviorally regulate body temperature, experiencing a fine-grained thermal environment.

    Purpose of the Study:

    • * To investigate the relationship between enzyme variability and enzyme function in two Anolis lizard species.
    • * To test if thermal environment differences correlate with enzyme heterozygosity levels.
    • * To determine which enzyme classes contribute to interspecific differences in heterozygosity.

    Main Methods:

    • * Electrophoretic surveys were conducted on enzyme variability in Anolis roquet and Anolis gundlachi.

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  • * Enzyme loci were categorized by substrate specificity (single- vs. multiple-substrate) and regulatory role (regulatory vs. nonregulatory).
  • * Heterozygosity levels were compared between the two species and across enzyme classes.
  • Main Results:

    • * Anolis gundlachi exhibited significantly higher overall enzyme heterozygosity compared to Anolis roquet.
    • * The elevated heterozygosity in A. gundlachi was primarily attributed to loci coding for multiple-substrate enzymes.
    • * The distinction between regulatory and nonregulatory enzymes did not explain the observed variability in heterozygosity.

    Conclusions:

    • * Enzyme heterozygosity levels are species-specific and influenced by ecological factors, such as thermal niche.
    • * Multiple-substrate enzymes may be more sensitive to environmental variation, leading to higher heterozygosity in species with less precise thermal regulation.
    • * Enzyme function, specifically substrate complexity, is a key factor in understanding patterns of genetic variability in lizards.