{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:42:14Z","timestamp":1759542134128,"version":"3.37.3"},"reference-count":37,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"Chinese National Natural Science Foundation","doi-asserted-by":"crossref","award":["31600086"],"award-info":[{"award-number":["31600086"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100007129","name":"Shandong province Natural Science Foundation","doi-asserted-by":"crossref","award":["ZR2016CQ06"],"award-info":[{"award-number":["ZR2016CQ06"]}],"id":[{"id":"10.13039\/501100007129","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Qingdao Agricultural University Scientific Research Foundation","award":["6631115052"],"award-info":[{"award-number":["6631115052"]}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2018,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The 1,125-bp\n            <jats:italic>mabB<\/jats:italic>\n            gene encoding 5-aminosalicylate (5ASA) 1,2-dioxygenase, a nonheme iron dioxygenase in the bicupin family that catalyzes the cleavage of the 5ASA aromatic ring to form\n            <jats:italic>cis<\/jats:italic>\n            -4-amino-6-carboxy-2-oxohexa-3,5-dienoate in the biodegradation of 3-aminobenzoate, was cloned from\n            <jats:named-content content-type=\"genus-species\">Comamonas<\/jats:named-content>\n            sp. strain QT12 and characterized. The deduced amino acid sequence of the enzyme has low sequence identity with that of other reported ring-cleaving dioxygenases. MabB was heterologously expressed in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            cells and purified as a His-tagged enzyme. The optimum pH and temperature for MabB are 8.0 and 10\u00b0C, respectively. Fe\n            <jats:sup>II<\/jats:sup>\n            is required for the catalytic activity of the purified enzyme. The apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            and\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            values of MabB for 5ASA are 52.0 \u00b1 5.6 \u03bcM and 850 \u00b1 33.2 U\/mg, respectively. The two oxygen atoms incorporated into the product of the MabB-catalyzed reaction are both from the dioxygen molecule. Both 5ASA and gentisate could be converted by MabB; however, the catalytic efficiency of MabB for 5ASA was much higher (\u223c70-fold) than that for gentisate. The\n            <jats:italic>mabB<\/jats:italic>\n            -disrupted mutant lost the ability to grow on 3-aminobenzoate, and\n            <jats:italic>mabB<\/jats:italic>\n            expression was higher when strain QT12 was cultivated in the presence of 3-aminobenzoate. Thus, 5ASA is the physiological substrate of MabB.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            For several decades, 5-aminosalicylate (5ASA) has been advocated as the drug mesalazine to treat human inflammatory bowel disease and considered the key intermediate in the xenobiotic degradation of many aromatic organic pollutants. 5ASA biotransformation research will help us elucidate the microbial degradation of these pollutants. Most studies have reported that gentisate 1,2-dioxygenases (GDOs) can convert 5ASA with significantly high activity; however, the catalytic efficiency of these enzymes for gentisate is much higher than that for 5ASA. This study showed that MabB can convert 5ASA to\n            <jats:italic>cis<\/jats:italic>\n            -4-amino-6-carboxy-2-oxohexa-3,5-dienoate, incorporating two oxygen atoms from the dioxygen molecule into the product. Unlike GDOs, MabB uses 5ASA instead of gentisate as the primary substrate.\n            <jats:italic>mabB<\/jats:italic>\n            is the first reported 5-aminosalicylate 1,2-dioxygenase gene.\n          <\/jats:p>","DOI":"10.1128\/jb.00395-17","type":"journal-article","created":{"date-parts":[[2017,10,17]],"date-time":"2017-10-17T00:40:32Z","timestamp":1508200832000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":5,"title":["Novel Gene Encoding 5-Aminosalicylate 1,2-Dioxygenase from Comamonas sp. Strain QT12 and Catalytic Properties of the Purified Enzyme"],"prefix":"10.1128","volume":"200","author":[{"given":"Hao","family":"Yu","sequence":"first","affiliation":[{"name":"Shandong Provincial Key Laboratory of Applied Mycology, College of Life Sciences, Qingdao Agricultural University, Qingdao, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shuxue","family":"Zhao","sequence":"additional","affiliation":[{"name":"Shandong Provincial Key Laboratory of Applied Mycology, College of Life Sciences, Qingdao Agricultural University, Qingdao, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lizhong","family":"Guo","sequence":"additional","affiliation":[{"name":"Shandong Provincial Key Laboratory of Applied Mycology, College of Life Sciences, Qingdao Agricultural University, Qingdao, People's Republic of 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