The extremo-α-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines

Bioorg Med Chem Lett. 2013 Feb 15;23(4):1087-90. doi: 10.1016/j.bmcl.2012.12.009. Epub 2012 Dec 20.

Abstract

The α-carbonic anhydrase (CA, EC 4.2.1.1) from the extremophilic bacterium Sulfurihydrogenibium azorense (SazCA) was recently shown to be the fastest CA known. Here we investigated this enzyme for its activation with a series of amino acids and amines. The best SazCA activators were D-Phe, L-DOPA, L- and D-Trp, dopamine and serotonin, which showed activation constants in the range of 3-23 nM. L- and D-His, L-Phe, L-Tyr, 2-pyridyl-methylamine and L-adrenaline were also effective activators (K(A)s in the range of 62-90 nM), whereas D-Dopa, D-Tyr and several heterocyclic amines showed activity in the micromolar range. The good thermal stability, robustness, very high catalytic activity and propensity to be activated by simple amino acids and amines, make SazCA a very interesting candidate for biomimetic CO(2) capture processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amines / chemistry
  • Amines / metabolism
  • Amino Acids / chemistry
  • Amino Acids / metabolism
  • Bacteria / enzymology*
  • Carbonic Anhydrases / chemistry*
  • Carbonic Anhydrases / metabolism*
  • Catalysis
  • Structure-Activity Relationship
  • Sulfur Compounds / metabolism

Substances

  • Amines
  • Amino Acids
  • Sulfur Compounds
  • Carbonic Anhydrases