Enzymatic resolution and pharmacological activity of the enantiomers of 3,5-dihydroxyphenylglycine, a metabotropic glutamate receptor agonist

3,5-Dihydroxyphenylglycine (3,5-DHPG) was resolved using an aminoacylase enzyme in solution, and the enantiomers characterised for ability to stimulate metabotropic glutamate receptor (mGluR) mediated phosphoinositide hydrolysis in rat hippocampus. The mGluR activity resided mainly in the (S) enantiomer, which should thus be a useful tool to further explore mGluR pharmacology and function.