{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T09:29:03Z","timestamp":1791278943223,"version":"4.1.0"},"reference-count":50,"publisher":"Microbiology Society","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,8,1]]},"abstract":"<jats:p>\n                    Rifamycin B biosynthesis by\n                    <jats:italic>Amycolatopsis mediterranei<\/jats:italic>\n                    S699 involves a number of unusual modification reactions in the formation of the unique polyketide backbone and decoration of the molecule. A number of genes believed to be involved in the tailoring of rifamycin B were investigated and the results confirmed that the formation of the naphthalene ring moiety of rifamycin takes place during the polyketide chain extension and is catalysed by Rif-Orf19, a 3-(3-hydroxyphenyl)propionate hydroxylase-like protein. The cytochrome P450-dependent monooxygenase encoded by\n                    <jats:italic>rif-orf5<\/jats:italic>\n                    is required for the conversion of the \u039412, 29 olefinic bond in the polyketide backbone of rifamycin W into the ketal moiety of rifamycin B. Furthermore, Rif-Orf3 may be involved in the regulation of rifamycin B production, as its knock-out mutant produced about 40\u200a% more rifamycin B than the wild-type. The work also revealed that many of the genes located in the cluster are not involved in rifamycin biosynthesis, but might be evolutionary remnants carried over from an ancestral lineage.\n                  <\/jats:p>","DOI":"10.1099\/mic.0.28138-0","type":"journal-article","created":{"date-parts":[[2005,8,3]],"date-time":"2005-08-03T17:13:13Z","timestamp":1123089193000},"page":"2515-2528","source":"Crossref","is-referenced-by-count":65,"title":["Identification of tailoring genes involved in the modification of the polyketide backbone of rifamycin B by Amycolatopsis mediterranei S699"],"prefix":"10.1099","volume":"151","author":[{"given":"Jun","family":"Xu","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eva","family":"Wan","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, OR 97331-3507, USA"},{"name":"Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chang-Joon","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heinz G.","family":"Floss","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taifo","family":"Mahmud","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, OR 97331-3507, USA"},{"name":"Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"6116","DOI":"10.1021\/bi010080z","article-title":"The loading module of rifamycin synthetase is an adenylation-thiolation didomain with substrate tolerance for substituted benzoates","volume":"40","author":"Admiraal","year":"2001","journal-title":"Biochemistry"},{"key":"R2","doi-asserted-by":"crossref","first-page":"5313","DOI":"10.1021\/bi0200312","article-title":"The loading and initial elongation modules of rifamycin synthetase collaborate to produce mixed aryl ketide products","volume":"41","author":"Admiraal","year":"2002","journal-title":"Biochemistry"},{"key":"R3","doi-asserted-by":"crossref","first-page":"2813","DOI":"10.1099\/00221287-145-10-2813","article-title":"Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441","volume":"145","author":"Arai","year":"1999","journal-title":"Microbiology"},{"key":"R4","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S1074-5521(98)90141-7","article-title":"Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699","volume":"5","author":"August","year":"1998","journal-title":"Chem Biol"},{"key":"R5","doi-asserted-by":"crossref","first-page":"6145","DOI":"10.1128\/JB.179.19.6145-6153.1997","article-title":"A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: cloning and characterization of the hpp operon","volume":"179","author":"Barnes","year":"1997","journal-title":"J Bacteriol"},{"key":"R6","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1126\/science.277.5331.1453","article-title":"The complete genome sequence of Escherichia coli K-12","volume":"277","author":"Blattner","year":"1997","journal-title":"Science"},{"key":"R7","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/S0092-8674(01)00286-0","article-title":"Structural mechanism for rifampicin inhibition of bacterial RNA polymerase","volume":"104","author":"Campbell","year":"2001","journal-title":"Cell"},{"key":"R8","doi-asserted-by":"crossref","first-page":"3149","DOI":"10.1073\/pnas.0537286100","article-title":"Type I polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis","volume":"100","author":"Cheng","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R9","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1021\/jm00250a005","article-title":"Oximes of 3-formylrifamycin SV. 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