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. 1980 Jan;141(1):137–143. doi: 10.1128/jb.141.1.137-143.1980

Bacillus cereus autolytic endoglucosaminidase active on cell wall peptidoglycan with N-unsubstituted glucosamine residues.

S Kawagishi, Y Araki, E Ito
PMCID: PMC293547  PMID: 6766437

Abstract

An autolytic glycosidase from a lysozyme-resistant strain of Bacillus cereus capable of cleaving the glycosidic linkages of N-unsubstituted glucosamine in the cell wall peptidoglycan was studied. This glycosidase activity, together with N-acetylmuramyl-L-alanine amidase activity, was found in an autolytic enzyme preparation obtained from the 20,000 x g precipitate fraction by means of autolysis followed by ammonium sulfate fractionation. The major saccharide fragments resulting from digestion of the untreated, non-N-acetylated, cell wall peptidoglycan of B. cereus with the autolytic enzyme preparation were identified as N-acetylmuramyl-glucosamine and its dimer. The peptidoglycan N-acetylated with acetic anhydride could also be digested with the same enzyme preparation, giving N-acetylmuramyl-N-acetylglucosamine and its dimer as the major saccharide fragments.

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Selected References

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

  1. Araki Y., Fukuoka S., Oba S., Ito E. Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls. Biochem Biophys Res Commun. 1971 Nov 5;45(3):751–758. doi: 10.1016/0006-291x(71)90481-5. [DOI] [PubMed] [Google Scholar]
  2. Araki Y., Ito E. A pathway of chitosan formation in Mucor rouxii. Enzymatic deacetylation of chitin. Eur J Biochem. 1975 Jun 16;55(1):71–78. doi: 10.1111/j.1432-1033.1975.tb02139.x. [DOI] [PubMed] [Google Scholar]
  3. Araki Y., Nakatani T., Nakayama K., Ito E. Occurrence of N-nonsubstituted glucosamine residues in peptidoglycan of lysozyme-resistant cell walls from Bacillus cereus. J Biol Chem. 1972 Oct 10;247(19):6312–6322. [PubMed] [Google Scholar]
  4. BROWDER H. P., ZYGMUNT W. A., YOUNG J. R., TAVORMINA P. A. LYSOSTAPHIN: ENZYMATIC MODE OF ACTION. Biochem Biophys Res Commun. 1965 Apr 23;19:383–389. doi: 10.1016/0006-291x(65)90473-0. [DOI] [PubMed] [Google Scholar]
  5. Hara S., Matsushima Y. Studies on the substrate specificity of egg white lysozyme. I. The N-acyl substituents in the substrate mucopolysaccharides. J Biochem. 1967 Jul;62(1):118–125. doi: 10.1093/oxfordjournals.jbchem.a128623. [DOI] [PubMed] [Google Scholar]
  6. Hayashi H., Araki Y., Ito E. Occurrence of glucosamine residues with free amino groups in cell wall peptidoglycan from bacilli as a factor responsible for resistance to lysozyme. J Bacteriol. 1973 Feb;113(2):592–598. doi: 10.1128/jb.113.2.592-598.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hedges A., Wolfe R. S. Extracellular enzyme from Myxobacter AL-1 that exhibits both beta-1,4-glucanase and chitosanase activites. J Bacteriol. 1974 Nov;120(2):844–853. doi: 10.1128/jb.120.2.844-853.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Iwata S., Kato K., Kotani S., Tamura T. Demonstration of endo-N-acetylglucosaminidase and endo-N-acetylmuramidase as impurities in a crude commercial preparation of -amylase from barley. Biken J. 1972 Sep;15(3):123–133. [PubMed] [Google Scholar]
  9. Kawagishi S., Araki Y., Ito E. A novel glycosidase, an endo-glucosaminidase active on the cell wall peptidoglycan with N-unsubstituted glucosamine residues. FEBS Lett. 1979 Jan 1;97(1):20–22. doi: 10.1016/0014-5793(79)80042-3. [DOI] [PubMed] [Google Scholar]
  10. Monaghan R. L., Eveleigh D. E., Tewari R. P., Reese E. T. Chitosanase, a novel enzyme. Nat New Biol. 1973 Sep 19;245(142):78–80. doi: 10.1038/newbio245078a0. [DOI] [PubMed] [Google Scholar]
  11. PARK J. T., JOHNSON M. J. A submicrodetermination of glucose. J Biol Chem. 1949 Nov;181(1):149–151. [PubMed] [Google Scholar]
  12. SALTON M. R. CHEMISTRY AND FUNCTION OF AMINO SUGARS AND DERIVATIVES. Annu Rev Biochem. 1965;34:143–174. doi: 10.1146/annurev.bi.34.070165.001043. [DOI] [PubMed] [Google Scholar]
  13. Tominaga Y., Tsujisaka Y. Purification and some enzymatic properties of the chitosanase from Bacillus R-4 which lyses Rhizopus cell walls. Biochim Biophys Acta. 1975 Nov 20;410(1):145–155. doi: 10.1016/0005-2744(75)90215-6. [DOI] [PubMed] [Google Scholar]
  14. Yoshimoto T., Tsuru D. Studies on bacteriolytic enzymes. II. Purification and some properties of two types of staphylolytic enzymes from Streptomyces griseus. J Biochem. 1972 Aug;72(2):379–390. doi: 10.1093/oxfordjournals.jbchem.a129913. [DOI] [PubMed] [Google Scholar]

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