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Chemical Compound Review

globomycin     12-butan-2-yl-19-hexyl-6-(1- hydroxyethyl)...

Synonyms: AGN-PC-0083UN, CHEMBL374030, LS-72696, CTK8D6770, AR-1C0589, ...
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Disease relevance of SF-1902A1

  • Cleavage of the pilin leader peptide is independent of known signal peptidases as demonstrated by pilin-processing profiles in Escherichia coli strains conditionally defective for production of leader peptidase or grown in the presence of the antibiotic globomycin [1].
  • The lipoprotein nature of FatB is supported by the fact that treatment of Vibrio anguillarum cells with globomycin, an inhibitor of the lipoprotein signal peptidase, results in the accumulation of a 38 kDa proFatB precursor protein [2].
  • In the current study, we showed that the product of the cloned gene could be labelled with palmitic acid, that it was subject to globomycin-sensitive processing, and that it was immunologically cross-reactive with azurin from Pseudomonas aeruginosa [3].
  • The use of the antibiotic globomycin in a minicell expression system and radioimmunoprecipitation analysis of Hib proteins intrinsically radiolabelled with [3H]-palmitate indicated that the 51K haemin-binding protein is a lipoprotein [4].
  • When the mycoplasma cell concentration was varied from 10(4) to 10(8) CFU/ml, the MICs of enrofloxacin and globomycin increased while those of the three other molecules remained essentially constant [5].

High impact information on SF-1902A1

  • Under the same conditions, globomycin does not prevent the attachment of palmitate or glycerol to the E. coli prolipoprotein but inhibits processing of the modified precursor to the mature lipoprotein [6].
  • The peptide antibiotic globomycin, which prevents processing of the E. coli prolipoprotein, severely inhibited the attachment of [3H]palmitate or [3H]glycerol to the 749/C enzyme (either in B. licheniformis 749/C or in E. coli), blocked the accumulation of penicillinase in the plasma membrane, and enhanced the formation of exoenzyme [6].
  • These results are in contrast with the lack of effect of globomycin on the RTEM-beta-lactamase of E. coli which has no detectable hydrophobic membrane form and was not labeled with palmitate or glycerol [6].
  • Overexpression, membrane fractionation, and metabolic labeling with [3H]palmitate demonstrated that Blc is indeed a globomycin-sensitive outer membrane lipoprotein [7].
  • Experiments with globomycin presented here also suggest that the primary precursor of EGL (ppEGL) has a 45-residue leader sequence but that only the first 19 residues of the leader sequence are removed by signal peptidase II during initial export across the inner membrane [8].

Chemical compound and disease context of SF-1902A1


Biological context of SF-1902A1

  • The plasmid pMT521, a subclone of pLC3-13 in pBR322, conferred on its host cells approximately 20 times overproduction of prolipoprotein signal peptidase and an extremely high level of resistance against globomycin [13].
  • The incorporation of exogenous [1-14C]palmitate into phosphatidylethanolamine in fadD mutants was inhibited by chloramphenicol and was depressed by preventing the acylation of the amino terminus of the lipoproteins with the antibiotic globomycin [14].
  • Three revertants were chosen in the present study which included the analysis of kinetics of lipoprotein maturation and the determination of globomycin sensitivity [15].
  • Lipoprotein fatty acids derived from the 1-position of phosphatidylethanolamine were resistant to hydroxylamine hydrolysis, and globomycin reduced the incorporation of exogenous [1-14C]palmitate into lipoproteins by 80% suggesting that this fatty acid is primarily attached to the amino terminus of the lipoprotein [14].
  • As predicted by the DNA sequence, the recombinant 15 kiloDalton immunogen labelled selectively with [3H]-palmitate, and globomycin inhibited processing of the precursor to the mature polypeptide [16].

Anatomical context of SF-1902A1


Associations of SF-1902A1 with other chemical compounds


Gene context of SF-1902A1


Analytical, diagnostic and therapeutic context of SF-1902A1

  • Immunoblotting analysis using the antibody against the 45-kDa protein revealed a 48-kDa precursor of the protein, which accumulated in the cyanobacterial cells treated with globomycin, an antibiotic that specifically inhibits cleavage of the signal peptide of lipoprotein precursors [28].
  • After treatment with globomycin, a significant amount of this modified precursor form accumulated and was degraded with time into smaller acylated proteins, but without release of the signal peptide [29].
  • SDS-PAGE analysis of cell proteins followed by immunolabeling ("Western blotting") and by crossed immunoelectrophoresis demonstrated that the cleavage of the prespiralin leader peptide was prevented by globomycin [22].


  1. Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria. Kaufman, M.R., Seyer, J.M., Taylor, R.K. Genes Dev. (1991) [Pubmed]
  2. Characterization and regulation of the expression of FatB, an iron transport protein encoded by the pJM1 virulence plasmid. Actis, L.A., Tolmasky, M.E., Crosa, L.M., Crosa, J.H. Mol. Microbiol. (1995) [Pubmed]
  3. Characterization of the neisserial lipid-modified azurin bearing the H.8 epitope. Woods, J.P., Dempsey, J.F., Kawula, T.H., Barritt, D.S., Cannon, J.G. Mol. Microbiol. (1989) [Pubmed]
  4. Molecular cloning, partial purification, and characterization of a haemin-binding lipoprotein from Haemophilus influenzae type b. Hanson, M.S., Hansen, E.J. Mol. Microbiol. (1991) [Pubmed]
  5. Activities of Antimicrobial Peptides and Synergy with Enrofloxacin against Mycoplasma pulmonis. Fassi Fehri, L., Wróblewski, H., Blanchard, A. Antimicrob. Agents Chemother. (2007) [Pubmed]
  6. Lipoprotein nature of Bacillus licheniformis membrane penicillinase. Nielsen, J.B., Caulfield, M.P., Lampen, J.O. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  7. Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins. Bishop, R.E., Penfold, S.S., Frost, L.S., Höltje, J.V., Weiner, J.H. J. Biol. Chem. (1995) [Pubmed]
  8. Evidence that extracellular export of the endoglucanase encoded by egl of Pseudomonas solanacearum occurs by a two-step process involving a lipoprotein intermediate. Huang, J.Z., Schell, M.A. J. Biol. Chem. (1990) [Pubmed]
  9. Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B. Dev, I.K., Ray, P.H. J. Biol. Chem. (1984) [Pubmed]
  10. Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein-dependent transport system. Schneider, R., Hantke, K. Mol. Microbiol. (1993) [Pubmed]
  11. Inhibition of secretion of a mutant lipoprotein across the cytoplasmic membrane by the wild-type lipoprotein of the Escherichia coli outer membrane. Lee, N., Yamagata, H., Inouye, M. J. Bacteriol. (1983) [Pubmed]
  12. Expression of the Serratia marcescens lipoproteins gene in Escherichia coli. Lee, N., Nakamura, K., Inouye, M. J. Bacteriol. (1981) [Pubmed]
  13. Isolation and characterization of an Escherichia coli clone overproducing prolipoprotein signal peptidase. Tokunaga, M., Loranger, J.M., Wu, H.C. J. Biol. Chem. (1983) [Pubmed]
  14. Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli. Jackowski, S., Rock, C.O. J. Biol. Chem. (1986) [Pubmed]
  15. Studies on the modification and processing of prolipoprotein in Escherichia coli. Effects of structural alterations in prolipoprotein on its maturation in wild type and lpp mutants. Tokunaga, H., Wu, H.C. J. Biol. Chem. (1984) [Pubmed]
  16. Lipid modification of the 15 kiloDalton major membrane immunogen of Treponema pallidum. Purcell, B.K., Swancutt, M.A., Radolf, J.D. Mol. Microbiol. (1990) [Pubmed]
  17. Existence of the bound form of prolipoprotein in Escherichia coli B cells treated with globomycin. Inukai, M., Takeuchi, M., Shimizu, K., Arai, M. J. Bacteriol. (1979) [Pubmed]
  18. Globomycin, a new peptide antibiotic with spheroplast-forming activity. II. Isolation and physico-chemical and biological characterization. Inukai, M., Nakajima, M., Osawa, M., Haneishi, T., Arai, M. J. Antibiot. (1978) [Pubmed]
  19. Secretion and lysophospholipase D activity of autotaxin by adipocytes are controlled by N-glycosylation and signal peptidase. Pradère, J.P., Tarnus, E., Grès, S., Valet, P., Saulnier-Blache, J.S. Biochim. Biophys. Acta (2007) [Pubmed]
  20. Association of the Rv0679c protein with lipids and carbohydrates in Mycobacterium tuberculosis/Mycobacterium bovis BCG. Matsuba, T., Suzuki, Y., Tanaka, Y. Arch. Microbiol. (2007) [Pubmed]
  21. Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes. Béven, L., Wróblewski, H. Res. Microbiol. (1997) [Pubmed]
  22. Inhibition of spiralin processing by the lipopeptide antibiotic globomycin. Béven, L., Le Hénaff, M., Fontenelle, C., Wróblewski, H. Curr. Microbiol. (1996) [Pubmed]
  23. A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome. Bouvier, J., Pugsley, A.P., Stragier, P. J. Bacteriol. (1991) [Pubmed]
  24. Isolation and characterization of a new globomycin-resistant dnaE mutant of Escherichia coli. Sakka, K., Watanabe, T., Beers, R., Wu, H.C. J. Bacteriol. (1987) [Pubmed]
  25. The plasmid R64 thin pilus identified as a type IV pilus. Kim, S.R., Komano, T. J. Bacteriol. (1997) [Pubmed]
  26. The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface. Fernandez, D., Dang, T.A., Spudich, G.M., Zhou, X.R., Berger, B.R., Christie, P.J. J. Bacteriol. (1996) [Pubmed]
  27. Molecular characterization of a conserved 20-kilodalton membrane-associated lipoprotein antigen of Helicobacter pylori. Kostrzynska, M., O'Toole, P.W., Taylor, D.E., Trust, T.J. J. Bacteriol. (1994) [Pubmed]
  28. Substrate-binding lipoprotein of the cyanobacterium Synechococcus sp. strain PCC 7942 involved in the transport of nitrate and nitrite. Maeda, S., Omata, T. J. Biol. Chem. (1997) [Pubmed]
  29. High-level expression of the colicin A lysis protein. Cavard, D., Howard, S.P., Lloubes, R., Lazdunski, C. Mol. Gen. Genet. (1989) [Pubmed]
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