Human carbonic anhydrases and carbonic anhydrase deficiencies

Annu Rev Biochem. 1995;64:375-401. doi: 10.1146/annurev.bi.64.070195.002111.

Abstract

Carbonic anhydrases (CAs I-VII) are products of a gene family that encodes seven isozymes and several homologous, CA- related proteins. All seven isozymes have been cloned, sequenced, and mapped, and the intron-exon organization of five genes established. They differ in subcellular localizations, being cytoplasmic (CA I, II, III, and VII), GPI-anchored to plasma membranes of specialized epithelial and endothelial cells (CA IV), in mitochondria (CA V), or in salivary secretions (CA VI). They also differ in kinetic properties, susceptibility to inhibitors, and tissue-specific distribution. Structural and kinetic studies of recombinant natural and mutant CAs have greatly increased our understanding of the structural requirements for catalysis. Studies of the effects of CA inhibitors over many years have implicated CAs in a variety of physiological processes. Analyses of human and animal CA deficiencies provide unique opportunities to understand the individual contributions of different isozymes to these processes.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carbonic Anhydrases / deficiency*
  • Carbonic Anhydrases / genetics
  • Carbonic Anhydrases / metabolism*
  • Chromosome Mapping
  • Disease Models, Animal
  • Female
  • Humans
  • Isoenzymes / metabolism
  • Macaca nemestrina
  • Male
  • Mice
  • Molecular Biology
  • Molecular Sequence Data
  • Molecular Structure
  • Sequence Homology, Amino Acid
  • Syndrome

Substances

  • Isoenzymes
  • Carbonic Anhydrases