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dc.contributor.authorLinnett, Paul E.
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):342-54. <a href="https://jb.asm.org/content/120/1/342/article-info" target="_blank" title="Link to article on publisher's site">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9193 (Linking)
dc.identifier.pmid4417383
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36497
dc.description.abstractIn synchronously sporulating cells of Bacillus sphaericus 9602, the specific activities of those enzymes specifically required for the synthesis of the UDP-N-acetyl-muramyl-pentapeptide precursor of vegetative cell wall peptidoglycan decay by 50% after the end of exponential cell division, probably as a consequence of dilution by newly synthesized protein. The meso-diaminopimelate ligase is the only new activity whose synthesis is required for synthesis of the nucleotide-pentapeptide precursor of spore cortex peptidoglycan. The addition of d-Ala-d-Ala to the nucleotide tripeptide is catalyzed by an enzyme present in both vegetative and sporulating cells, which apparently does not discriminate between lysine- and diaminopimelate-containing acceptors. The activities of the l-Ala and d-Ala-d-Ala ligases and of the d-Ala-d-Ala synthetase increases in parallel with the appearance of the diaminopimelate ligase, indicating coordinate derepression and suggesting operon-like organization of the appropriate structural genes.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=4417383&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.titleCell wall polymers of Bacillus sphaericus: activities of enzymes involved in peptidoglycan precursor synthesis during sporulation
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume120
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1059&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/59
dc.identifier.contextkey14823808
refterms.dateFOA2022-08-23T16:26:08Z
html.description.abstract<p>In synchronously sporulating cells of Bacillus sphaericus 9602, the specific activities of those enzymes specifically required for the synthesis of the UDP-N-acetyl-muramyl-pentapeptide precursor of vegetative cell wall peptidoglycan decay by 50% after the end of exponential cell division, probably as a consequence of dilution by newly synthesized protein. The meso-diaminopimelate ligase is the only new activity whose synthesis is required for synthesis of the nucleotide-pentapeptide precursor of spore cortex peptidoglycan. The addition of d-Ala-d-Ala to the nucleotide tripeptide is catalyzed by an enzyme present in both vegetative and sporulating cells, which apparently does not discriminate between lysine- and diaminopimelate-containing acceptors. The activities of the l-Ala and d-Ala-d-Ala ligases and of the d-Ala-d-Ala synthetase increases in parallel with the appearance of the diaminopimelate ligase, indicating coordinate derepression and suggesting operon-like organization of the appropriate structural genes.</p>
dc.identifier.submissionpathmaps_pubs/59
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages342-54


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