Stereospecificity of Phenylyruvate Tautomerase

Abstract
It was shown by 1H NMR spectroscopy that phenylpyruvate tautomerase [EC 5.3.2.1] from beef kidney catalyzes the stereospecific exchange of one of the enantiotopic 3-H atoms in the side-chain of the substrate with solvent protons, the rate of spontaneous exchange being slow under physiological conditions. Using monodeuterated phenylpyruvate of known absolute configuration it was shown that the tautomerase removes specifically the 3-pro-R H atom of the substrate. The circular dichroism spectra of the 2 enantiomeric 3-phenyl-[3-2H]pyruvates were determined. Some implications of these findings for the investigation of the metabolism of aromatic amino acids are discussed.

This publication has 10 references indexed in Scilit: