Carbonic anhydrase activators. The first activation study of a coral secretory isoform with amino acids and amines

Bioorg Med Chem. 2010 Mar 15;18(6):2300-2303. doi: 10.1016/j.bmc.2010.01.059. Epub 2010 Feb 4.

Abstract

The activity of the coral Stylophora pystillata secretory carbonic anhydrase STPCA has been tested in presence of amino acids and amines. All the investigated compounds showed a positive, activating effect on k(cat) and have been separated in weak (K(A) in the range of 21-126 microM), medium (10.1-19 microM) and strong enzyme activators (K(A) of 0.18-3.21 microM). D-DOPA was found to be the best coral enzyme activator, with an activation constant K(A) of 0.18 microM. This enhancement of STPCA activity, as well as previous enzyme inhibition results, might now be tested on living organisms to better understand the role played by these enzymes in the coral calcification processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amines / chemistry
  • Amines / pharmacology*
  • Amino Acids / chemistry
  • Amino Acids / pharmacology*
  • Animals
  • Anthozoa / enzymology*
  • Anthozoa / metabolism
  • Carbonic Anhydrases / metabolism*
  • Enzyme Activation / drug effects
  • Humans
  • Isoenzymes / metabolism
  • Kinetics
  • Molecular Structure
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Amines
  • Amino Acids
  • Isoenzymes
  • Carbonic Anhydrases