{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,6]],"date-time":"2024-08-06T20:16:06Z","timestamp":1722975366717},"reference-count":31,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2013,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Since the peptidoglycan isolated from\n            <jats:named-content content-type=\"genus-species\">Mycobacterium<\/jats:named-content>\n            spp. is refractory to commercially available murolytic enzymes, possibly due to the presence of various modifications found on this peptidoglycan, the utility of a mycobacteriophage-derived murolytic enzyme was assessed for an analysis of peptidoglycan from mycobacteria. We cloned, expressed, and purified the\n            <jats:italic>lysA<\/jats:italic>\n            gene product, a protein with homology to known peptidoglycan-degrading amidases, from bacteriophage Ms6. The recombinant protein was shown to cleave the bond between\n            <jats:sc>l<\/jats:sc>\n            -Ala and\n            <jats:sc>d<\/jats:sc>\n            -muramic acid of muramyl pentapeptide and to release up to 70% of the diaminopimelic acid present in the isolated mycobacterial cell wall. In contrast to lysozyme, which, in culture, inhibits the growth of both\n            <jats:named-content content-type=\"genus-species\">Mycobacterium smegmatis<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">Mycobacterium tuberculosis<\/jats:named-content>\n            , LysA had no effect on the growth of either species. However, the enzyme is useful for solubilizing the peptide chains of isolated mycobacterial peptidoglycan for analysis. The data indicate that the stem peptides from\n            <jats:named-content content-type=\"genus-species\">M. smegmatis<\/jats:named-content>\n            are heavily amidated, containing few free carboxylic acids, regardless of the cross-linking status.\n          <\/jats:p>","DOI":"10.1128\/aem.02263-12","type":"journal-article","created":{"date-parts":[[2012,11,17]],"date-time":"2012-11-17T05:52:23Z","timestamp":1353131543000},"page":"768-773","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["Mycobacteriophage Ms6 LysA: a Peptidoglycan Amidase and a Useful Analytical Tool"],"prefix":"10.1128","volume":"79","author":[{"given":"Sebabrata","family":"Mahapatra","sequence":"first","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]},{"given":"Charles","family":"Piechota","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]},{"given":"Filipa","family":"Gil","sequence":"additional","affiliation":[{"name":"Centro de Patog\u00e9nese Molecula, Unidade dos Retrovirus e Infec\u00e7\u00f5es Associadas, Faculdade de Farm\u00e1cia, Universidade de Lisboa, Lisbon, Portugal"}]},{"given":"Yufang","family":"Ma","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"},{"name":"Department of Biochemistry and Molecular Biology, Dalian Medical University, Dalian, People's Republic of China"}]},{"given":"Hairong","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"},{"name":"Beijing Tuberculosis and Thoracic Tumor Institute, Beijing, People's Republic of China"}]},{"given":"Michael S.","family":"Scherman","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]},{"given":"Victoria","family":"Jones","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]},{"suffix":"Jr.","given":"Martin S.","family":"Pavelka","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, New York, USA"}]},{"given":"Jose","family":"Moniz-Pereira","sequence":"additional","affiliation":[{"name":"Centro de Patog\u00e9nese Molecula, Unidade dos Retrovirus e Infec\u00e7\u00f5es Associadas, Faculdade de Farm\u00e1cia, Universidade de Lisboa, Lisbon, Portugal"}]},{"given":"Madalena","family":"Pimentel","sequence":"additional","affiliation":[{"name":"Centro de Patog\u00e9nese Molecula, Unidade dos Retrovirus e Infec\u00e7\u00f5es Associadas, Faculdade de Farm\u00e1cia, Universidade de Lisboa, Lisbon, Portugal"}]},{"given":"Michael R.","family":"McNeil","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]},{"given":"Dean C.","family":"Crick","sequence":"additional","affiliation":[{"name":"Department of Microbiology Immunology and Pathology, Colorado State University, Fort Collins, Colorado, USA"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)39211-7"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/9781555817657.ch18"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.187.8.2747-2757.2005"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00982-07"},{"key":"e_1_3_3_6_2","first-page":"249","article-title":"Studies on peptides, glycopeptides and antigenic polysaccharide-glycopeptide complexes isolated from an L-11 enzyme lysate of the cell walls of Mycobacterium tuberculosis strain H37Rv","volume":"13","author":"Kotani S","year":"1970","unstructured":"KotaniS YanagidaI KatoK MatsudaT. 1970. 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