{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T12:15:52Z","timestamp":1784031352388,"version":"3.55.0"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2008,10,15]],"date-time":"2008-10-15T00:00:00Z","timestamp":1224028800000},"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":[[2008,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Cyanase catalyzes the decomposition of cyanate into CO\n            <jats:sub>2<\/jats:sub>\n            and ammonium, with carbamate as an unstable intermediate. The cyanase of\n            <jats:italic>Pseudomonas pseudoalcaligenes<\/jats:italic>\n            CECT5344 was negatively regulated by ammonium and positively regulated by cyanate, cyanide, and some cyanometallic complexes. Cyanase activity was not detected in cell extracts from cells grown with ammonium, even in the presence of cyanate. Nevertheless, a low level of cyanase activity was detected in nitrogen-starved cells. The\n            <jats:italic>cyn<\/jats:italic>\n            gene cluster of\n            <jats:italic>P. pseudoalcaligenes<\/jats:italic>\n            CECT5344 was cloned and analyzed. The\n            <jats:italic>cynA, cynB<\/jats:italic>\n            , and\n            <jats:italic>cynD<\/jats:italic>\n            genes encode an ABC-type transporter, the\n            <jats:italic>cynS<\/jats:italic>\n            gene codes for the cyanase, and the\n            <jats:italic>cynF<\/jats:italic>\n            gene encodes a novel \u03c3\n            <jats:sup>54<\/jats:sup>\n            -dependent transcriptional regulator which is not present in other bacterial\n            <jats:italic>cyn<\/jats:italic>\n            gene clusters. The CynS protein was expressed in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            and purified by following a simple and rapid protocol. The\n            <jats:italic>P. pseudoalcaligenes<\/jats:italic>\n            cyanase showed an optimal pH of 8.5\u00b0C and a temperature of 65\u00b0C. An insertion mutation was generated in the\n            <jats:italic>cynS<\/jats:italic>\n            gene. The resulting mutant was unable to use cyanate as the sole nitrogen source but showed the same resistance to cyanate as the wild-type strain. These results, in conjunction with the induction pattern of the enzymatic activity, suggest that the enzyme has an assimilatory function. Although the induction of cyanase activity in cyanide-degrading cells suggests that some cyanate may be generated from cyanide, the\n            <jats:italic>cynS<\/jats:italic>\n            mutant was not affected in its ability to degrade cyanide, which unambiguously indicates that cyanate is not a central metabolite in cyanide assimilation.\n          <\/jats:p>","DOI":"10.1128\/aem.00916-08","type":"journal-article","created":{"date-parts":[[2008,8,15]],"date-time":"2008-08-15T20:26:05Z","timestamp":1218831965000},"page":"6280-6288","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":55,"title":["Characterization of the\n            <i>Pseudomonas pseudoalcaligenes<\/i>\n            CECT5344 Cyanase, an Enzyme That Is Not Essential for Cyanide Assimilation"],"prefix":"10.1128","volume":"74","author":[{"given":"Vi\u0301ctor M.","family":"Luque-Almagro","sequence":"first","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mari\u0301a-J.","family":"Huertas","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lara P.","family":"Sa\u0301ez","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel Marti\u0301nez","family":"Luque-Romero","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Conrado","family":"Moreno-Vivia\u0301n","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco","family":"Castillo","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Dolores","family":"Rolda\u0301n","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular, Universidad de Co\u0301rdoba, Edificio Severo Ochoa, 1a Planta, Campus de Rabanales, E-14071 Co\u0301rdoba, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rafael","family":"Blasco","sequence":"additional","affiliation":[{"name":"Departamento de Bioqui\u0301mica y Biologi\u0301a Molecular y Gene\u0301tica, Facultad de Veterinaria, Universidad de Extremadura, Avenida de la Universidad SN, E-10071 Ca\u0301ceres, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"S135","volume":"39","year":"1998","unstructured":"Aichi, M., I Nishida, and T. Omata. 1998. Molecular cloning and characterization of a cDNA encoding cyanase from Arabidopsis thaliana. Plant Cell. Physiol. Suppl.39:S135.","journal-title":"Plant Cell. Physiol. 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