[Aminoacylase from Streptoverticillium microorganisms: stereo- and substrate specificity].
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.
D000581:Amidohydrolases / Q000378:metabolism*; D006868:Hydrolysis; D007930:Leucine / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D013237:Stereoisomerism; D013306:Streptomycetaceae / Q000201:enzymology*; D013379:Substrate Specificity; D014364:Tryptophan / Q000378:metabolism
D010649:Phenylalanine; D014364:Tryptophan; D008715:Methionine; D000581:Amidohydrolases; C019672:aminoacylase I; D007930:Leucine
Aminoatsilaza mikroorganizmov iz roda Streptoverticillium: izuchenie stereo- i substratnoĭ spetsifichnosti.