{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,21]],"date-time":"2023-11-21T21:44:59Z","timestamp":1700603099808},"reference-count":25,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2014,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Corallopyronin A is a promising\n            <jats:italic>in vivo<\/jats:italic>\n            active antibiotic, currently undergoing preclinical evaluation. This myxobacterial compound interferes with a newly identified drug target site, i.e., the switch region of the bacterial DNA-dependent RNA-polymerase (RNAP). Since this target site differs from that of known RNAP inhibitors such as the rifamycins, corallopyronin A shows no cross-resistance with other antibacterial agents. Corallopyronin A is a polyketide synthase- and nonribosomal peptide synthetase-derived molecule whose structure and biosynthesis is distinguished by several peculiarities, such as the unusual vinyl carbamate functionality whose formation involves carbonic acid as an unprecedented C1-starter unit. Using\n            <jats:italic>in vitro<\/jats:italic>\n            experiments the nature of this starter molecule was revealed to be the methyl ester of carbonic acid. Biochemical investigations showed that methylation of carbonic acid is performed by the\n            <jats:italic>O<\/jats:italic>\n            -methyltransferase CorH. These experiments shed light on the biosynthesis of the Eastern chain of \u03b1-pyrone antibiotics such as corallopyronin A.\n          <\/jats:p>","DOI":"10.1128\/aac.01894-13","type":"journal-article","created":{"date-parts":[[2013,11,26]],"date-time":"2013-11-26T03:28:07Z","timestamp":1385436487000},"page":"950-956","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":7,"title":["Function of the Loading Module in CorI and of the\n            <i>O<\/i>\n            -Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A"],"prefix":"10.1128","volume":"58","author":[{"given":"Till F.","family":"Sch\u00e4berle","sequence":"first","affiliation":[{"name":"Institute for Pharmaceutical Biology, University of Bonn, Bonn, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mahsa","family":"Mir Mohseni","sequence":"additional","affiliation":[{"name":"Institute for 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