Journal
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume 28, Issue 2, Pages 267-277Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/14756366.2012.737323
Keywords
Human carbonic anhydrase; annotation; classification; comparison; thermostability; industrial applications
Funding
- University of Florida
- HHMI Science for Life
- National Institutes of Health [GM25154]
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Carbonic anhydrases (CAs, EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible interconversion of CO2 and HCO3-. Of the 15 isoforms of human (h) alpha-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 Zn2+ 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.
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