Cell wall polymers of Bacillus sphaericus: activities of enzymes involved in peptidoglycan precursor synthesis during sporulation
dc.contributor.author | Linnett, Paul E. | |
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):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.issn | 0021-9193 (Linking) | |
dc.identifier.pmid | 4417383 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/36497 | |
dc.description.abstract | 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. | |
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=4417383&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 | Cell wall polymers of Bacillus sphaericus: activities of enzymes involved in peptidoglycan precursor synthesis during sporulation | |
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=1059&context=maps_pubs&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/maps_pubs/59 | |
dc.identifier.contextkey | 14823808 | |
refterms.dateFOA | 2022-08-23T16:26:08Z | |
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.submissionpath | maps_pubs/59 | |
dc.contributor.department | Department of Microbiology and Physiological Systems | |
dc.contributor.department | Department of Microbiology | |
dc.source.pages | 342-54 |