从枯草芽孢杆菌的D-丙氨酸羧肽酶中分离青霉素结合肽。
Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
作者信息
Georgopapadakou N, Hammarström S, Strominger J L
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009.
Abstract
The D-alanine carboxypeptidase of B. subtilis is a membrane-bound enzyme which is inhibited by penicillins and binds them covalently. The enzyme has been labeled with [14C]- or [35S]penicillin. After tryptic or Pronase digestion of the labeled, denatured, reduced, and carboxymethylated enzyme, a radioactive peptide was isolated in each case. The amino acid compositions of these two peptides are reported. The Pronase peptide was a subset of the tryptic peptide. Neither contained a cysteine residue and the only amino acid in the Pronase peptide to which the penicillin could be bound was a serine residue.
摘要
枯草芽孢杆菌的D-丙氨酸羧肽酶是一种膜结合酶，它会受到青霉素的抑制并与其共价结合。该酶已用[14C] - 或[35S]青霉素进行标记。在用胰蛋白酶或链霉蛋白酶消化标记的、变性的、还原的和羧甲基化的酶后，每种情况下都分离出了一种放射性肽段。报告了这两种肽段的氨基酸组成。链霉蛋白酶肽段是胰蛋白酶肽段的一个子集。两者都不含有半胱氨酸残基，链霉蛋白酶肽段中唯一能结合青霉素的氨基酸是一个丝氨酸残基。
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