The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines

Bioorg Med Chem Lett. 2012 Oct 15;22(20):6324-7. doi: 10.1016/j.bmcl.2012.08.088. Epub 2012 Aug 30.

Abstract

The α-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its activation with a series of amino acids and amines. D-His, L-Phe, L-Tyr, L- and D-Trp were the most effective SspCA activators, with activation constants in the range of 1-12 nM, whereas L-His, L/D-DOPA, D-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (K(A) in the range of 37 nM-0.97 μM). The least effective SspCA activator was d-Phe (K(A) of 5.13 μM). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO(2) capture processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amines / metabolism
  • Amino Acids / metabolism
  • Carbon Dioxide / metabolism
  • Carbonic Anhydrases / metabolism*
  • Enzyme Activation
  • Gram-Negative Chemolithotrophic Bacteria / enzymology*
  • Kinetics

Substances

  • Amines
  • Amino Acids
  • Carbon Dioxide
  • Carbonic Anhydrases