Appearance of gamma-D-glutamyl-(L) meso-diaminopimealate peptidoglycan hydrolase during sporulation in Bacillus sphaericus
dc.contributor.author | Guinand, M. | |
dc.contributor.author | Michel, G. | |
dc.contributor.author | Tipper, Donald J. | |
dc.date | 2022-08-11T08:09:18.000 | |
dc.date.accessioned | 2022-08-23T16:26:07Z | |
dc.date.available | 2022-08-23T16:26:07Z | |
dc.date.issued | 1974-10-01 | |
dc.date.submitted | 2019-06-27 | |
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.issn | 0021-9193 (Linking) | |
dc.identifier.pmid | 4417809 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/36496 | |
dc.description.abstract | 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. | |
dc.language.iso | en_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.rights | Copyright © 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.subject | Bacteriology | |
dc.subject | Microbiology | |
dc.subject | Physiology | |
dc.title | Appearance of gamma-D-glutamyl-(L) meso-diaminopimealate peptidoglycan hydrolase during sporulation in Bacillus sphaericus | |
dc.type | Journal Article | |
dc.source.journaltitle | Journal of bacteriology | |
dc.source.volume | 120 | |
dc.source.issue | 1 | |
dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1058&context=maps_pubs&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/maps_pubs/58 | |
dc.identifier.contextkey | 14823805 | |
refterms.dateFOA | 2022-08-23T16:26:07Z | |
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.submissionpath | maps_pubs/58 | |
dc.contributor.department | Department of Microbiology and Physiological Systems | |
dc.contributor.department | Department of Microbiology | |
dc.source.pages | 173-84 |