title: Structural annotation of human carbonic anhydrases.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
authors.forename: Mayank
authors.initials: M
authors.lastname: Aggarwal
authors.forename: Christopher D
authors.initials: CD
authors.lastname: Boone
authors.forename: Bhargav
authors.initials: B
authors.lastname: Kondeti
authors.forename: Robert
authors.initials: R
authors.lastname: McKenna
mesh_terms: D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D007527:Isoenzymes; D002256:Carbonic Anhydrases