UDP-N-acetylmuramylpentapeptide as acceptor in murein biosynthesis in 
Escherichia coli membranes and ether-permeabilized cells

Kraus, W; Glauner, B; Höltje, J-V

doi:10.1128/jb.162.3.1000-1004.1985

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

UDP-N-acetylmuramylpentapeptide as acceptor in murein biosynthesis in Escherichia coli membranes and ether-permeabilized cells

MPS-Authors

/persons/resource/persons293603

Kraus, W
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons285495

Glauner, B
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons284215

Höltje, J-V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Kraus, W., Glauner, B., & Höltje, J.-V. (1985). UDP-N-acetylmuramylpentapeptide as acceptor in murein biosynthesis in Escherichia coli membranes and ether-permeabilized cells. Journal of Bacteriology, 162(3), 1000-1004. doi:10.1128/jb.162.3.1000-1004.1985.

引用: https://hdl.handle.net/21.11116/0000-000D-EA82-8

要旨

Two widely used in vitro systems of Escherichia coli capable of synthesizing murein were evaluated by using high-pressure liquid chromatography for murein analysis. Comparison of the composition of murein synthesized by either a membrane preparation or ether-treated cells with native murein revealed that both in vitro systems failed to synthesize murein that was identical to murein formed in vivo. Furthermore, neither system attached the lipoprotein to the murein. Ether-treated cells, however, were superior to the membrane preparation in catalyzing the formation of the remarkable A2pm-A2pm cross-linkage. In both systems an atypical transpeptidation reaction was found to take place in which exogenously supplied UDP-N-acetylmuramylpentapeptide was directly linked to the murein without participation of the bactoprenol lipid carrier. The direct transpeptidation yields preferentially trimeric peptide bridges with the UDP-linked muramylpentapeptide serving as the acceptor.