链霉菌K15 D-丙氨酰-D-丙氨酸羧肽酶/青霉素结合蛋白。活性位点及N端区域序列。
The Streptomyces K15 DD-peptidase/penicillin-binding protein. Active site and sequence of the N-terminal region.
作者信息
Leyh-Bouille M, Van Beeumen J, Renier-Pirlot S, Joris B, Nguyen-Distèche M, Ghuysen J M
机构信息
Service de Microbiologie, Université de Liège, Institut de Chimie, Belgium.
出版信息
Biochem J. 1989 Jun 1;260(2):601-4. doi: 10.1042/bj2600601.
Abstract
The N-terminal region of the Streptomyces K15 DD-peptidase/penicillin-binding protein shows high homology with that of other penicillin-interactive proteins or domains. The active-site serine residue of the conserved tetrad Ser-Xaa-Xaa-Lys occurs at position 35. There is no indication for the presence of a signal peptide or an N-terminal hydrophobic sequence, suggesting that the Streptomyces K15 enzyme is probably anchored to the membrane by a C-terminal peptide segment.
摘要
链霉菌K15 DD-肽酶/青霉素结合蛋白的N端区域与其他青霉素相互作用蛋白或结构域的N端区域具有高度同源性。保守的四联体Ser-Xaa-Xaa-Lys中的活性位点丝氨酸残基位于第35位。没有迹象表明存在信号肽或N端疏水序列，这表明链霉菌K15酶可能通过C端肽段锚定在膜上。
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引用本文的文献
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本文引用的文献
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