Kinetic and anion inhibition studies of a β-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis

Bioorg Med Chem Lett. 2013 Mar 15;23(6):1626-30. doi: 10.1016/j.bmcl.2013.01.087. Epub 2013 Jan 30.


Several β-carbonic anhydrases (CAs, EC are present in all land plants examined thus far. Here we report the first detailed biochemical characterization of one such isoform, FbiCA 1, from the C4 plant Flaveria bidentis, which was cloned, purified and characterized as recombinant protein. FbiCA 1 has an interesting CO2 hydrase catalytic activity (kcat of 1.2×10(5) and kcat/Km of 7.5×10(6)M(-1)×s(-1)) and was moderately inhibited by most simple/complex inorganic anions. Potent FbiCA 1 inhibitors were also detected, such as trithiocarbonate, diethyldithiocarbamate, sulfamide, sulfamic acid, phenylboronic acid and phenylarsonic acid (KIs in the range of 4-60μM). Such inhibitors may be used as tools to better understand the role of various β-CA isoforms in photosynthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anions / chemistry*
  • Anions / metabolism
  • Carbon Dioxide / metabolism
  • Carbonic Anhydrase Inhibitors / chemistry*
  • Carbonic Anhydrase Inhibitors / metabolism
  • Carbonic Anhydrases / chemistry*
  • Carbonic Anhydrases / classification
  • Carbonic Anhydrases / metabolism
  • Flaveria / enzymology*
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Phylogeny
  • Protein Isoforms / chemistry
  • Protein Isoforms / classification
  • Protein Isoforms / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism


  • Anions
  • Carbonic Anhydrase Inhibitors
  • Protein Isoforms
  • Recombinant Proteins
  • Carbon Dioxide
  • Carbonic Anhydrases