ISOLATION OF PENICILLIN-BINDING PEPTIDE FROM D-ALANINE CARBOXYPEPTIDASE OF BACILLUS-SUBTILIS
ISOLATION OF PENICILLIN-BINDING PEPTIDE FROM D-ALANINE CARBOXYPEPTIDASE OF BACILLUS-SUBTILIS
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DOI：
10.1073/pnas.74.3.1009
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发表时间：
1977-01-01
影响因子：
11.1
通讯作者：
STROMINGER, JL
中科院分区：
文献类型：
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作者：
GEORGOPAPADAKOU, N;HAMMARSTROM, S;STROMINGER, JL
枯草芽孢杆菌的 D-丙氨酸羧肽酶是一种膜结合酶，可被青霉素抑制并与青霉素共价结合。该酶用[14C]-或[35S]青霉素标记。对标记的、变性的、还原的和羧甲基化的酶进行胰蛋白酶或链霉蛋白酶消化后，在每种情况下分离出放射性肽。报道了这两种肽的氨基酸组成。链霉蛋白酶肽是胰蛋白酶肽的一个子集。两者都不含有半胱氨酸残基，并且链霉蛋白酶肽中唯一可以与青霉素结合的氨基酸是丝氨酸残基。
The D-alanine carboxypeptidase of B. subtilis is a membrane-bound enzyme which is inhibited by penicillins and binds them covalently. The enzyme was 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 2 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.