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Bacterial Lipid II Analogs: Novel In Vitro Substrates for Mammalian Oligosaccharyl Diphosphodolichol Diphosphatase (DLODP) Activities. | LitMetric

AI Article Synopsis

  • Mammalian protein glycosylation requires a specific oligosaccharide transfer in the endoplasmic reticulum, and disrupted pathways can lead to the formation of oligosaccharyl phosphates (OSP).
  • The study aimed to create a fluorescence-based assay to investigate DLO diphosphatase activity, overcoming challenges posed by the lack of suitable non-radioactive substrates.
  • The research demonstrated that mouse liver extracts can hydrolyze a fluorescent bacterial lipid, producing GM5P, indicating that similar enzymes may process both bacterial lipids and mammalian DLO.

Article Abstract

Mammalian protein -glycosylation requires the transfer of an oligosaccharide containing 2 residues of N-acetylglucosamine, 9 residues of mannose and 3 residues of glucose (GlcMan GlcNAc) from GlcManGlcNAc-diphospho (PP)-dolichol (DLO) onto proteins in the endoplasmic reticulum (ER). Under some pathophysiological conditions, DLO biosynthesis is perturbed, and truncated DLO is hydrolyzed to yield oligosaccharyl phosphates (OSP) via unidentified mechanisms. DLO diphosphatase activity (DLODP) was described in vitro, but its characterization is hampered by a lack of convenient non-radioactive substrates. Our objective was to develop a fluorescence-based assay for DLO hydrolysis. Using a vancomycin-based solid-phase extraction procedure coupled with thin layer chromatography (TLC) and mass spectrometry, we demonstrate that mouse liver membrane extracts hydrolyze fluorescent bacterial lipid II (LII: GlcNAc-MurNAc(dansyl-pentapeptide)-PP-undecaprenol) to yield GlcNAc-MurNAc(dansyl-pentapeptide)-P (GM5P). GM5P production by solubilized liver microsomal proteins shows similar biochemical characteristics to those reported for human hepatocellular carcinoma HepG2 cell DLODP activity. To conclude, we show, for the first time, hydrolysis of lipid II by a eukaryotic enzyme. As LII and DLO are hydrolyzed by the same, or closely related, enzymes, fluorescent lipid II analogs are convenient non-radioactive substrates for investigating DLODP and DLODP-like activities.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6600155PMC
http://dx.doi.org/10.3390/molecules24112135DOI Listing

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