Evolution of Structure and Function in the Carbonic Anhydrase Isozymes of Mammals

  • R. E. Tashian
  • D. Hewett-Emmett
  • S. K. Stroup
  • M. Goodman
  • Y.-S. L. Yu
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Comparative studies on the primary structures of the carbonic anhydrase isozymes, designated CA I and CA II, from a number of mammlian species have shown that nearly one half (46%) of the amino acid residues at homologous positions in these isozymes has remained invariant (cf. Tashian, 1977). Because of this high degree of sequence homology between the two carbonic anhydrase isozymes and the fact that the three-dimensional structures of human CA I and CA II are very similar (Kannan et al., 1975; Liljas et al., 1972; Notstrand et al., 1974), it is clear that the structural genes for these isozymes arose from the same ancestral gene. These isozymes are known to differ, sometimes markedly, in their stabilities to heat and denaturing reagents, specific activities, and inhibition by cyclic sulfonamides, halides, and anions (Cf. Lindskog et al., 1971; Maren, 1976; Tashian, 1977). Thus, some critical changes must have evolved in the structures (active site residues?) of these isozymes to account for the observed functional differences (Notstrand et al., 1974; Kannan et al., 1977). Recently, a third isozyme of carbonic anhydrase has been reported, which we have designated CA III, from mammalian skeletal muscle (Holmes, 1977; Koester et al., 1977; Tashian, 1977, 1978; Tashian et al., 1978) some of whose properties differ strikingly from those of CA I and II. For example, the CO2 hydratase and esterase activities and sulfonamide binding affinity of the CA III isozymes are much lower than those of the CA I and II isozymes, especially the esterase activity and sulfon­amide binding affinity (Holmes, 1977; Koester et al., 1977; Tashian et al., 1978; Carter et al., 1979). In addition, the conformational properties of CA III appear to be uniquely different from CA I and CA II (Koester and Noltmann, 1979).

Keywords

Codon Halide Transferase Nitrophenyl Phosphorylase 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1980

Authors and Affiliations

  • R. E. Tashian
    • 1
  • D. Hewett-Emmett
    • 1
  • S. K. Stroup
    • 1
  • M. Goodman
    • 2
  • Y.-S. L. Yu
    • 1
  1. 1.Department of Human GeneticsUniversity of Michigan Medical SchoolAnn ArborUSA
  2. 2.Department of AnatomyWayne State University School of MedicineDetroitUSA

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