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Minami A, Ishibashi S, Ikeda K, et al. Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues. FEBS Open Bio. 2013;3:231-6doi: 10.1016/j.fob.2013.05.002.
Minami, A., Ishibashi, S., Ikeda, K., Ishitsubo, E., Hori, T., Tokiwa, H., Taguchi, R., Ieno, D., Otsubo, T., Matsuda, Y., Sai, S., Inada, M., & Suzuki, T. (2013). Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues. FEBS open bio, 3231-6. https://doi.org/10.1016/j.fob.2013.05.002
Minami, Akira, et al. "Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues." FEBS open bio vol. 3 (2013): 231-6. doi: https://doi.org/10.1016/j.fob.2013.05.002
Minami A, Ishibashi S, Ikeda K, Ishitsubo E, Hori T, Tokiwa H, Taguchi R, Ieno D, Otsubo T, Matsuda Y, Sai S, Inada M, Suzuki T. Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues. FEBS Open Bio. 2013 May 29;3:231-6. doi: 10.1016/j.fob.2013.05.002. Print 2013. PMID: 23772399; PMCID: PMC3678298.
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FEBS Open Bio. 2013 May 29;3:231-6. doi: 10.1016/j.fob.2013.05.002. Print 2013.

Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues.

FEBS open bio

Akira Minami, Sayaka Ishibashi, Kiyoshi Ikeda, Erika Ishitsubo, Takanori Hori, Hiroaki Tokiwa, Risa Taguchi, Daisuke Ieno, Tadamune Otsubo, Yukino Matsuda, Saki Sai, Mari Inada, Takashi Suzuki

Affiliations

  1. Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan.

PMID: 23772399 PMCID: PMC3678298 DOI: 10.1016/j.fob.2013.05.002

Abstract

In a comparison of sialidase activities toward N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we found that Salmonella typhimurium LT2 sialidase (STSA) hardly cleaved 4-methylumbelliferyl Neu5Gc (4MU-Neu5Gc). The k cat/K m value of STSA for 4MU-Neu5Gc was found to be 110 times lower than that for 4-methylumbelliferyl Neu5Ac (4MU-Neu5Ac). Additionally, STSA had remarkably weak ability to cleave α2-3-linked-Neu5Gc contained in gangliosides and equine erythrocytes. In silico analysis based on first-principle calculations with transition-state analogues suggested that the binding affinity of Neu5Gc2en is 14.3 kcal/mol more unstable than that of Neu5Ac2en. The results indicated that STSA preferentially cleaves Neu5Ac residues rather than Neu5Gc residues, which is important for anyone using this enzyme to cleave α2-3-linked sialic acids.

Keywords: 4MU, 4-methylumbelliferone; 4MU-Neu5Ac, 4-methylumbelliferyl N-acetylneuraminic acid; 4MU-Neu5Gc; 4MU-Neu5Gc, 4-methylumbelliferyl N-glycolylneuraminic acid; AUSA, Arthrobacter ureafaciens sialidase; Boc, tert-butoxycarbonyl; CPSA, Clostridium perfingens sialidase; DANA, 2,3-dehydro-2-deoxy-N-acetylneuraminic acid; DMAP, 4-dimethylaminopyridine; DMB, 1,2-diamino-4,5-methylenedioxybenzene; Docking simulations; E. coli, Escherichia coli; HPLC, high-performance liquid chromatography; MDSA, Macrobdella decora sialidase; N-glycolylneuraminic acid; N.D., not detected; Neu5Ac, N-acetylneuraminic acid; Neu5Gc, N-glycolylneuraminic acid; PBS, phosphate buffered saline; STSA, Salmonella typhimurium LT2 sialidase; Salmonella typhimurium LT2 sialidase; Sia, sialic acid; Sialic acid; Substrate specificity; THF, tetrahydrofuran; VCSA, Vibrio cholerae sialidase; rt, room temperature

References

  1. Glycoconj J. 2006 Jul;23(5-6):277-90 - PubMed
  2. J Biol Chem. 1965 Sep;240(9):3501-6 - PubMed
  3. Glycoconj J. 1992 Oct;9(5):235-40 - PubMed
  4. Biochem J. 1981 Aug 1;197(2):293-9 - PubMed
  5. Virology. 1997 Jan 20;227(2):493-9 - PubMed
  6. J Biochem. 1989 Dec;106(6):1086-9 - PubMed
  7. Biochemistry. 1969 Dec;8(12):5082-8 - PubMed
  8. J Biol Chem. 1994 Jul 22;269(29):18821-6 - PubMed
  9. PLoS One. 2010 Dec 09;5(12):e15556 - PubMed
  10. Glycoconj J. 1998 Aug;15(8):769-75 - PubMed
  11. Structure. 1994 Jun 15;2(6):535-44 - PubMed
  12. J Mol Graph Model. 2000 Jun;18(3):283-9, 307-8 - PubMed
  13. Glycoconj J. 2012 May;29(4):231-7 - PubMed
  14. Anal Biochem. 2000 Jun 1;281(2):193-201 - PubMed
  15. J Vet Med Sci. 1994 Apr;56(2):375-7 - PubMed
  16. Biochimie. 2007 Nov;89(11):1396-408 - PubMed
  17. J Biochem. 1980 Feb;87(2):639-43 - PubMed
  18. J Mol Biol. 1996 Jun 7;259(2):264-80 - PubMed
  19. J Biochem. 1979 Nov;86(5):1573-85 - PubMed
  20. J Biol Chem. 1979 Aug 25;254(16):7845-54 - PubMed
  21. J Biochem. 1991 Sep;110(3):462-7 - PubMed
  22. J Biol Chem. 1985 Feb 10;260(3):1362-5 - PubMed
  23. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9852-6 - PubMed
  24. J Med Microbiol. 1978 Aug;11(3):269-80 - PubMed
  25. Glycoconj J. 2006 Feb;23(1-2):101-6 - PubMed
  26. Curr Opin Struct Biol. 2009 Oct;19(5):507-14 - PubMed
  27. ACS Chem Biol. 2012 Sep 21;7(9):1509-14 - PubMed
  28. Glycoconj J. 2009 Apr;26(3):231-45 - PubMed
  29. Eur J Biochem. 1993 Dec 15;218(3):797-806 - PubMed
  30. J Biol Chem. 1983 Jan 25;258(2):876-81 - PubMed
  31. Biochim Biophys Acta. 1983 Apr 28;744(2):121-6 - PubMed
  32. FEBS Lett. 1997 Mar 10;404(2-3):192-6 - PubMed
  33. Neuroimage. 2011 Sep 1;58(1):34-40 - PubMed

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