Open AccessStereospecificity of Phenylyruvate Tautomerase
Author(s) -
RÉTEY Jànos,
BARTLV Knut,
RIPP Engelbert,
HULL William E.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11247.x
Subject(s) - stereospecificity , chemistry , substrate (aquarium) , enantiomer , circular dichroism , stereochemistry , enzyme , chirality (physics) , enantiomeric excess , biochemistry , catalysis , chiral symmetry , enantioselective synthesis , biology , nambu–jona lasinio model , physics , quantum mechanics , quark , ecology
1 By 1 H nuclear magnetic resonance spectroscopy it has been shown that phenylpyruvate tautomerase from beef kidney catalyses 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. 2 Using monodeuterated phenylpyruvate of known absolute configuration it has been shown that the tautomerase removes specifically the 3‐ pro ‐ R hydrogen atom of the substrate. 3 The circular dichroism spectra of the two enantiomeric 3‐phenyl‐[3‐ 2 H]pyruvates have been determined. 4 Some implications of these findings for the investigation of the metabolism of aromatic amino acids are discussed.