Structural annotation of human carbonic anhydrases

J Enzyme Inhib Med Chem. 2013 Apr;28(2):267-77. doi: 10.3109/14756366.2012.737323. Epub 2012 Nov 9.

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible interconversion of CO(2) and HCO(3)(-). Of the 15 isoforms of human (h) α-CA, 12 are catalytic (hCAs I-IV, VA, VB, VI, VII, IX, XII-XIV). The remaining three acatalytic isoforms (hCAs VIII, X and XI) lack the active site Zn(2+) and are referred to as CA-related proteins (CA-RPs); however, their function remains elusive. Overall these isoforms are very similar to each other in structure but they differ in their expression and distribution. The favourable properties of hCA II such as fast kinetics, easy expression and purification, high solubility and intermediate heat resistance have made it an attractive candidate for numerous industrial applications. This review highlights the structural similarity and stability comparison among hCAs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Carbonic Anhydrases / chemistry*
  • Carbonic Anhydrases / isolation & purification
  • Carbonic Anhydrases / metabolism
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Protein Conformation

Substances

  • Isoenzymes
  • Carbonic Anhydrases