Aminoacylase from Streptoverticillium microorganisms: stereo- and substrate specificity
Skvortsova, E.E.; Galaev, I.I.; Nys, P.S.; Shviadas, V.K.; Savitskaia, E.M.
Biokhimiia 49(4): 547-550
1984
ISSN/ISBN: 0320-9725 PMID: 6733158 Document Number: 226047
The stereo- and substrate specificity of a new aminoacylase from Streptoverticillium microorganisms was studied. The enzyme effectively hydrolyzes acetyl derivatives of aliphatic (methionine, leucine) and aromatic (phenylglycine, phenylalanine, tryptophan) amino acids. The L-enanthiomer of acetylphenylglycine is hydrolyzed by aminoacylase 8000 times more effectively than the D-enanthiomer. A procedure for determination of the enanthioselectivity of aminoacylases was elaborated. This procedure is designed for a detection and assessment of contaminations of the N-acetyl derivative of one enanthiomer by another enanthiomer of the amino acid, as well as of the degree of racemization of the substrate during hydrolysis of acetyl derivatives of D-amino acids.