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dc.contributor.authorGuinand, M.
dc.contributor.authorMichel, G.
dc.contributor.authorTipper, Donald J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:07Z
dc.date.available2022-08-23T16:26:07Z
dc.date.issued1974-10-01
dc.date.submitted2019-06-27
dc.identifier.citation<p>J Bacteriol. 1974 Oct;120(1):173-84. <a href="https://jb.asm.org/content/120/1/173/article-info" target="_blank" title="Link to article on publisher's website">Link to article on publisher's website</a></p>
dc.identifier.issn0021-9193 (Linking)
dc.identifier.pmid4417809
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36496
dc.description.abstractParticulate preparations from sporulating cells of Bacillus sphaericus 9602 contained an endopeptidase activity that hydrolyzed the gamma-d-glutamyl-(l)meso-diaminopimelic acid linkages found in the spore cortical peptidoglycan of this organism. Diaminopimelic acid did not occur in the vegetative cell wall peptidoglycan, and the gamma-d-glutamyl-l-lysine linkages found in this polymer were not hydrolyzed by the endopeptidase. The endopeptidase hydrolyzed (X)-l-alanyl-gamma-d-glutamyl-(l)meso-diaminopimelyl(l)-d-alanyl-d-alanine only after removal of the terminal d-alanine residue. The preparations contained an acyl-d-alanyl-d-alanine carboxypeptidase I activity which converted such pentapeptides into substrates for the endopeptidase and which was inhibited 50% by 4 x 10(-7) M benzylpenicillin. This activity also hydrolyzed the analogous pentapeptide substrates containing l-lysine. The preparations also contained an acyl-l-lysyl-d-alanine carboxypeptidase II activity that was not active on the meso-diaminopimelic acid-containing analogue. Neither this activity nor the endopeptidase was inhibited by 10(-3) M benzylpenicillin. The specificities of the carboxypeptidases were consistent with the exclusive presence of l-lysine C-termini in the vegetative peptidoglycan and of meso-diaminopimelyl-d-alanine C-termini in the spore cortical peptidoglycan of B. sphaericus 9602.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=4417809&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 1974, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at https://journals.asm.org/content/copyright-transfer-and-supplemental-material-license-agreement-2017.
dc.subjectBacteriology
dc.subjectMicrobiology
dc.subjectPhysiology
dc.titleAppearance of gamma-D-glutamyl-(L) meso-diaminopimealate peptidoglycan hydrolase during sporulation in Bacillus sphaericus
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume120
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1058&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/58
dc.identifier.contextkey14823805
refterms.dateFOA2022-08-23T16:26:07Z
html.description.abstract<p>Particulate preparations from sporulating cells of Bacillus sphaericus 9602 contained an endopeptidase activity that hydrolyzed the gamma-d-glutamyl-(l)meso-diaminopimelic acid linkages found in the spore cortical peptidoglycan of this organism. Diaminopimelic acid did not occur in the vegetative cell wall peptidoglycan, and the gamma-d-glutamyl-l-lysine linkages found in this polymer were not hydrolyzed by the endopeptidase. The endopeptidase hydrolyzed (X)-l-alanyl-gamma-d-glutamyl-(l)meso-diaminopimelyl(l)-d-alanyl-d-alanine only after removal of the terminal d-alanine residue. The preparations contained an acyl-d-alanyl-d-alanine carboxypeptidase I activity which converted such pentapeptides into substrates for the endopeptidase and which was inhibited 50% by 4 x 10(-7) M benzylpenicillin. This activity also hydrolyzed the analogous pentapeptide substrates containing l-lysine. The preparations also contained an acyl-l-lysyl-d-alanine carboxypeptidase II activity that was not active on the meso-diaminopimelic acid-containing analogue. Neither this activity nor the endopeptidase was inhibited by 10(-3) M benzylpenicillin. The specificities of the carboxypeptidases were consistent with the exclusive presence of l-lysine C-termini in the vegetative peptidoglycan and of meso-diaminopimelyl-d-alanine C-termini in the spore cortical peptidoglycan of B. sphaericus 9602.</p>
dc.identifier.submissionpathmaps_pubs/58
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages173-84


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