马杜拉放线菌R39胞外DD-羧肽酶-转肽酶中的青霉素结合位点。
The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.
作者信息
Duez C, Joris B, Frère J M, Ghuysen J M, Van Beeumen J
出版信息
Biochem J. 1981 Jan 1;193(1):83-6. doi: 10.1042/bj1930083.
Abstract
Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70 h at 37 degrees C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].
摘要
先前在苄青霉素与马杜拉放线菌R39的胞外DD - 羧肽酶 - 转肽酶之间形成的复合物经热变性和链霉蛋白酶降解后，产生一种七肽H - 亮氨酸 - 脯氨酸 - 丙氨酸 - 丝氨酸 - 天冬酰胺 - 甘氨酸 - 缬氨酸 - 羟基，其中苄青霉素酰基以酯键连接到丝氨酸残基上。这种连接非常不稳定，其水解会导致苄青霉素酸的释放。相比之下，天然的苄青霉素酰 - 酶复合物非常稳定（在37℃下半衰期为70小时），其分解是通过结合的苄青霉素酰基的断裂进行的[富阿德、弗雷尔、居伊森、迪兹和岩津保（1976年）《生物化学杂志》155卷，623 - 629页]。
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