{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T04:31:12Z","timestamp":1768451472185,"version":"3.49.0"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2011,10,15]],"date-time":"2011-10-15T00:00:00Z","timestamp":1318636800000},"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":["J Bacteriol"],"published-print":{"date-parts":[[2011,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A new pathway of molinate mineralization has recently been described. Among the five members of the mixed culture able to promote such a process,\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Gulosibacter molinativorax<\/jats:named-content>\n            ON4\n            <jats:sup>T<\/jats:sup>\n            has been observed to promote the initial breakdown of the herbicide into ethanethiol and azepane-1-carboxylate. In the current study, the gene encoding the enzyme responsible for molinate hydrolysis was identified and heterologously expressed, and the resultant active protein was purified and characterized. Nucleotide sequence analysis revealed that the gene encodes a 465-amino-acid protein of the metal-dependent hydrolase A subfamily of the amidohydrolase superfamily with a predicted molecular mass of 50.9 kDa. Molinate hydrolase shares the highest amino acid sequence identity (48 to 50%) with phenylurea hydrolases of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Arthrobacter globiformis<\/jats:named-content>\n            and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Mycobacterium brisbanense<\/jats:named-content>\n            . However, in contrast to previously described members of the metal-dependent hydrolase A subfamily, molinate hydrolase contains cobalt as the only active-site metal.\n          <\/jats:p>","DOI":"10.1128\/jb.05054-11","type":"journal-article","created":{"date-parts":[[2011,8,13]],"date-time":"2011-08-13T02:21:19Z","timestamp":1313202079000},"page":"5810-5816","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Gulosibacter molinativorax ON4\n            <sup>T<\/sup>\n            Molinate Hydrolase, a Novel Cobalt-Dependent Amidohydrolase"],"prefix":"10.1128","volume":"193","author":[{"given":"M\u00e1rcia","family":"Duarte","sequence":"first","affiliation":[{"name":"LEPAE-Departamento de Engenharia Qu\u00edmica, Faculdade de Engenharia, Universidade do Porto, Porto, Portugal"}]},{"given":"Frederico","family":"Ferreira-da-Silva","sequence":"additional","affiliation":[{"name":"IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal"}]},{"given":"Heinrich","family":"L\u00fcnsdorf","sequence":"additional","affiliation":[{"name":"Department of Vaccinology and Applied Microbiology, HZI-Helmholtz Centre for Infection Research, Braunschweig, Germany"}]},{"given":"Howard","family":"Junca","sequence":"additional","affiliation":[{"name":"Microbial Interactions and Processes Research Group, HZI-Helmholtz Centre for Infection Research, Braunschweig, Germany"}]},{"given":"Lu\u00eds","family":"Gales","sequence":"additional","affiliation":[{"name":"IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal"},{"name":"ICBAS-Instituto de Ci\u00eancias Biom\u00e9dicas Abel Salazar, Porto, Portugal"}]},{"given":"Dietmar H.","family":"Pieper","sequence":"additional","affiliation":[{"name":"Microbial Interactions and Processes Research Group, HZI-Helmholtz Centre for Infection Research, Braunschweig, Germany"}]},{"given":"Olga C.","family":"Nunes","sequence":"additional","affiliation":[{"name":"LEPAE-Departamento de Engenharia Qu\u00edmica, Faculdade de Engenharia, Universidade do Porto, Porto, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.2007\/015297-0"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1462-2920.2003.00492.x"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1101\/gr.3.2.85"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1006\/rtph.1997.1082"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.watres.2005.11.016"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2005.09.086"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2105-5-113"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2008.04.022"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.180.18.4781-4789.1998"},{"key":"e_1_3_3_12_2","first-page":"348","article-title":"Transformation of ordram by microorganisms","volume":"3","author":"Golovleva L. 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