Skvortsova E E, Galaev I Iu, Nys P S, Shviadas V K, Savitskaia E M
Biokhimiia. 1984 Apr;49(4):547-50.
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.
研究了来自轮枝链霉菌微生物的一种新型氨酰基酶的立体特异性和底物特异性。该酶能有效水解脂肪族氨基酸（蛋氨酸、亮氨酸）和芳香族氨基酸（苯甘氨酸、苯丙氨酸、色氨酸）的乙酰衍生物。乙酰苯甘氨酸的L-对映体被氨酰基酶水解的效率比D-对映体高8000倍。阐述了一种测定氨酰基酶对映体选择性的方法。该方法旨在检测和评估一种氨基酸对映体的N-乙酰衍生物被另一种对映体污染的情况，以及D-氨基酸乙酰衍生物水解过程中底物的消旋程度。
