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  • 标题:Complex Lipid Requirements for Detergent-Solubilized Phosphoacetylmuramyl-Pentapeptide Translocase from Micrococcus luteus
  • 本地全文:下载
  • 作者:Jay N. Umbreit ; Jack L. Strominger
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1972
  • 卷号:69
  • 期号:7
  • 页码:1972-1974
  • DOI:10.1073/pnas.69.7.1972
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Phospho-MurNAc-pentapeptide translocase activity in the membrane of M. luteus was lost upon addition of the detergent, Triton X-100, but could be restored by addition of lipid fractions to the assay. By assay in the presence of lipid, the activity of the Triton-solubilized enzyme could be measured. The synthesis of C55-isoprenyl-P-P-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide required C55-isoprenyl-P, and was stimulated by a neutral lipid. The exchange reaction of UDP-MurNAc-pentapeptide with UMP required a polar lipid fraction, but the reaction was not affected by C55-isoprenyl-P or the neutral lipid. Thus, measurement of activity of the detergent-solubilized enzyme requires addition of three lipids, the lipid substrate (C55-isoprenyl-P), the neutral lipid, and a polar lipid.
  • 关键词:Triton X-100 ; cell wall synthesis ; membrane-bound ; C55-isoprenyl alcohol ; enzyme
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