{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T18:55:34Z","timestamp":1762541734239},"reference-count":50,"publisher":"American Society for Microbiology","issue":"18","license":[{"start":{"date-parts":[[2008,9,15]],"date-time":"2008-09-15T00:00:00Z","timestamp":1221436800000},"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":[[2008,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Nucleoside 5\u2032-diphosphate-X hydrolases are interesting enzymes to study due to their varied activities and structure-function relationships and the roles they play in the disposal, assimilation, and modulation of the effects of their substrates. Few of these enzymes with a preference for CDP-alcohols are known. In\n            <jats:italic>Yersinia intermedia<\/jats:italic>\n            suspensions prepared from cultures on Columbia agar with 5% sheep blood, we found a CDP-alcohol hydrolase liberated to Triton X-100-containing medium. Growth at 25\u00b0C was deemed optimum in terms of the enzyme-activity yield. The purified enzyme also displayed 5\u2032-nucleotidase, UDP-sugar hydrolase, and dinucleoside-polyphosphate hydrolase activities. It was identified as the protein product (UshA\n            <jats:sub>Yi<\/jats:sub>\n            ) of the\n            <jats:italic>Y. intermedia ushA<\/jats:italic>\n            gene (\n            <jats:italic>ushA<\/jats:italic>\n            <jats:sub>Yi<\/jats:sub>\n            ) by its peptide mass fingerprint and by PCR cloning and expression to yield active enzyme. All those activities, except CDP-alcohol hydrolase, have been shown to be the properties of UshA of\n            <jats:italic>Escherichia coli<\/jats:italic>\n            (UshA\n            <jats:sub>Ec<\/jats:sub>\n            ). Therefore, UshA\n            <jats:sub>Ec<\/jats:sub>\n            was expressed from an appropriate plasmid and tested for CDP-alcohol hydrolase activity. UshA\n            <jats:sub>Ec<\/jats:sub>\n            and UshA\n            <jats:sub>Yi<\/jats:sub>\n            behaved similarly. Besides being the first study of a UshA enzyme in the genus\n            <jats:italic>Yersinia<\/jats:italic>\n            , this work adds CDP-alcohol hydrolase to the spectrum of UshA activities and offers a novel perspective on these proteins, which are viewed here for the first time as highly efficient enzymes with\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>cat<\/jats:sub>\n            <jats:italic>\/K<\/jats:italic>\n            <jats:sub>\n              <jats:italic>m<\/jats:italic>\n            <\/jats:sub>\n            ratios near the theoretical maximum level of catalytic activities. The results are discussed in the light of the known structures of UshA\n            <jats:sub>Ec<\/jats:sub>\n            conformers and the respective homology models constructed for UshA\n            <jats:sub>Yi<\/jats:sub>\n            , and also in relation to possible biological functions. Interestingly, every\n            <jats:italic>Yersinia<\/jats:italic>\n            species with a sequenced genome contains an intact\n            <jats:italic>ushA<\/jats:italic>\n            gene, except\n            <jats:italic>Y. pestis<\/jats:italic>\n            , which in all its sequenced biovars contains a\n            <jats:italic>ushA<\/jats:italic>\n            gene inactivated by frameshift mutations.\n          <\/jats:p>","DOI":"10.1128\/jb.00658-08","type":"journal-article","created":{"date-parts":[[2008,7,19]],"date-time":"2008-07-19T00:54:50Z","timestamp":1216428890000},"page":"6153-6161","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["CDP-Alcohol Hydrolase, a Very Efficient Activity of the 5\u2032-Nucleotidase\/UDP-Sugar Hydrolase Encoded by the\n            <i>ushA<\/i>\n            Gene of\n            <i>Yersinia intermedia<\/i>\n            and\n            <i>Escherichia coli<\/i>"],"prefix":"10.1128","volume":"190","author":[{"given":"Isabel","family":"Alves-Pereira","sequence":"first","affiliation":[{"name":"Grupo de Enzimologi\u0301a, Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain"},{"name":"Departamento de Qui\u0301mica, Universidade de E\u0301vora, E\u0301vora, Portugal"}]},{"given":"Jose\u0301","family":"Canales","sequence":"additional","affiliation":[{"name":"Grupo de Enzimologi\u0301a, Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain"}]},{"given":"Alicia","family":"Cabezas","sequence":"additional","affiliation":[{"name":"Grupo de Enzimologi\u0301a, Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain"}]},{"given":"Paloma","family":"Marti\u0301n Cordero","sequence":"additional","affiliation":[{"name":"Servicio de Microbiologi\u0301a, Complejo Hospitalario Universitario de Badajoz, Servicio Extremen\u0303o de Salud, Badajoz, Spain"}]},{"given":"Mari\u0301a Jesu\u0301s","family":"Costas","sequence":"additional","affiliation":[{"name":"Grupo de Enzimologi\u0301a, Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain"}]},{"given":"Jose\u0301 Carlos","family":"Cameselle","sequence":"additional","affiliation":[{"name":"Grupo de Enzimologi\u0301a, Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Medicina, Universidad de Extremadura, Badajoz, Spain"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.116.2.957-964.1973"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1046\/j.1365-2958.2002.02940.x","volume":"44","year":"2002","unstructured":"Bengoechea, J. 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