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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Jul;69(7):1972–1974. doi: 10.1073/pnas.69.7.1972

Complex Lipid Requirements for Detergent-Solubilized Phosphoacetylmuramyl-Pentapeptide Translocase from Micrococcus luteus

Jay N Umbreit 1, Jack L Strominger 1
PMCID: PMC426843  PMID: 4340168

Abstract

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.

Keywords: Triton X-100, cell wall synthesis, membrane-bound, C55-isoprenyl alcohol, enzyme

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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