{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,12]],"date-time":"2026-07-12T02:48:07Z","timestamp":1783824487100,"version":"3.55.0"},"reference-count":19,"publisher":"American Society for Microbiology","issue":"16","license":[{"start":{"date-parts":[[2014,8,15]],"date-time":"2014-08-15T00:00:00Z","timestamp":1408060800000},"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":[[2014,8,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The peptidyl nucleoside arginomycin is active against Gram-positive bacteria and fungi but displays much lower toxicity to mice than its analog blasticidin S. It features a rare amino acid, \u03b2-methylarginine, which is attached to the deoxyhexose moiety via a 4\u2032-aminoacyl bond. We here report cloning of the complete biosynthetic gene cluster for arginomycin from\n            <jats:named-content content-type=\"genus-species\">Streptomyces arginensis<\/jats:named-content>\n            NRRL 15941. Among the 14 putative essential open reading frames,\n            <jats:italic>argM<\/jats:italic>\n            , encoding an aspartate aminotransferase (AAT), and adjacent\n            <jats:italic>argN<\/jats:italic>\n            , encoding an\n            <jats:italic>S<\/jats:italic>\n            -adenosyl methionine (SAM)-dependent methyltransferase, are coupled to catalyze arginine and yield \u03b2-methylarginine in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            . Purified ArgM can transfer the \u03b1-amino group of\n            <jats:sc>l<\/jats:sc>\n            -arginine to \u03b1-ketoglutaric acid to give glutamate and thereby converts\n            <jats:sc>l<\/jats:sc>\n            -arginine to 5-guanidino-2-oxopentanoic acid, which is methylated at the C-3 position by ArgN to form 5-guanidino-3-methyl-2-oxopentanoic acid. Iteratively, ArgM specifically catalyzes transamination from the donor\n            <jats:sc>l<\/jats:sc>\n            -aspartate to the resulting 5-guanidino-3-methyl-2-oxopentanoic acid, generating \u03b2-methylarginine. The complete and concise biosynthetic pathway for the rare and bioactive amino acid revealed by this study may pave the way for the production of \u03b2-methylarginine either by enzymatic conversion or by engineered living cells.\n          <\/jats:p>","DOI":"10.1128\/aem.01172-14","type":"journal-article","created":{"date-parts":[[2014,6,7]],"date-time":"2014-06-07T08:26:22Z","timestamp":1402129582000},"page":"5021-5027","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":21,"title":["Biosynthesis of the \u03b2-Methylarginine Residue of Peptidyl Nucleoside Arginomycin in Streptomyces arginensis NRRL 15941"],"prefix":"10.1128","volume":"80","author":[{"given":"Jun","family":"Feng","sequence":"first","affiliation":[{"name":"State Key Laboratory of Microbial Metabolism and School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, China"},{"name":"National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention, Key Laboratory of Parasite and Vector Biology, Ministry of Health, and WHO Collaborating Centre for Malaria, Schistosomiasis and Filariasis, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Wu","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Metabolism and School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jie","family":"Gao","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Metabolism and School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhigui","family":"Xia","sequence":"additional","affiliation":[{"name":"National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention, Key Laboratory of Parasite and Vector Biology, Ministry of Health, and WHO Collaborating Centre for Malaria, Schistosomiasis and Filariasis, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zixin","family":"Deng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Metabolism and School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinyi","family":"He","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Metabolism and School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.7164\/antibiotics.40.750"},{"key":"e_1_3_3_3_2","first-page":"65","article-title":"Effect of blasticidin S on protein synthesis of Pyricularia oryzae","volume":"17","author":"Huang KT","year":"1964","unstructured":"HuangKTMisatoTAsuyamaH. 1964. Effect of blasticidin S on protein synthesis of Pyricularia oryzae. J. Antibiot. (Tokyo) 17:65\u201370.","journal-title":"J. Antibiot. (Tokyo)"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00225a033"},{"key":"e_1_3_3_5_2","first-page":"1292","article-title":"Studies on the biosynthesis of blasticidin S. Part I. Precursors of blasticidin S biosynthesis","volume":"32","author":"Seto H","year":"1968","unstructured":"SetoHFurihataKYoneharaH. 1968. Studies on the biosynthesis of blasticidin S. Part I. Precursors of blasticidin S biosynthesis. J. Antibiot. (Tokyo) 32:1292\u20131298.","journal-title":"J. Antibiot. 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Tyrosine aminotransferase: a transaminase among others? Cell. Mol. Biol. 38:95\u2013114.","journal-title":"Cell. Mol. Biol."},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00726-013-1508-y"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2002.03108.x"}],"container-title":["Applied and Environmental Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AEM.01172-14","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AEM.01172-14","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,23]],"date-time":"2022-02-23T02:51:49Z","timestamp":1645584709000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AEM.01172-14"}},"subtitle":[],"editor":[{"given":"R. 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