{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T05:37:22Z","timestamp":1791178642141,"version":"4.1.0"},"reference-count":45,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[2013,6,5]],"date-time":"2013-06-05T00:00:00Z","timestamp":1370390400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2013,7]]},"abstract":"<jats:sec><jats:label\/><jats:p>We examined six <jats:italic><jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>rabidopsis\u00a0thaliana<\/jats:italic> genes from the DJ\u20101\/PfpI superfamily for similarity to the recently characterized bacterial and animal glyoxalases. Based on their sequence similarities, the six genes were classified into two sub\u2010groups consisting of homologs of the human <jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1<\/jats:italic> gene and the <jats:italic>PH1704<\/jats:italic> gene of <jats:italic>Pyrococcus\u00a0horikoshii<\/jats:italic>. Unlike the homologs from other species, all the <jats:italic>A.\u00a0thaliana<\/jats:italic> genes have two tandem domains, which may have been created by gene duplication. The six AtDJ\u20101 proteins (a\u2013f) were expressed in <jats:italic>Escherichia\u00a0coli<\/jats:italic> for enzymatic assays with glyoxals. The DJ\u20101d protein, which belongs to the PH1704 sub\u2010group, exhibits the highest activity against methylglyoxal and glyoxal, and <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values of 0.10 and 0.27\u00a0m<jats:sc>m<\/jats:sc> were measured for these two substrates, respectively, while the corresponding <jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub> values were 1700 and 2200\u00a0min<jats:sup>\u22121<\/jats:sup>, respectively. The DJ\u20101a and DJ\u20101b glyoxalases exhibited higher specificity towards glyoxal. The other three proteins have either no or extremely low activity for glyoxals. For the DJ\u20101d enzyme, the residues, Cys120\/313 and Glu19\/212 at the active site and His121\/314 and Glu94\/287 at the oligomeric interface were mutated to alanines. As in other enzymes characterized to date, mutation of either the Cys or the Glu residues of the active site completely abolished enzyme activity, whereas mutation of the interface residues produced a variable decrease in activity. DJ\u20101d differs from its animal and bacterial homologs with respect to the configuration of its catalytic residues and the oligomeric property of the enzyme. When the wild\u2010type DJ\u20101d enzyme was expressed in <jats:italic>E.\u00a0coli<\/jats:italic>, the bacteria became resistant to glyoxals.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Nucleotide sequence data are available in the GenBank database under accession numbers <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_112361\">NM_112361<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1a<\/jats:italic>), <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_104206\">NM_104206<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1b<\/jats:italic>), <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_119563\">NM_119563<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1c<\/jats:italic>), <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_111140\">NM_111140<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1d<\/jats:italic>), <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_090959.1\">NM_090959.1<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1e<\/jats:italic>) and <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.ncbi.nlm.nih.gov\/protein\/NM_115317.5\">NM_115317.5<\/jats:ext-link> (<jats:italic>DJ<\/jats:italic>\u2010<jats:italic>1f<\/jats:italic>).<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12321","type":"journal-article","created":{"date-parts":[[2013,5,8]],"date-time":"2013-05-08T07:25:52Z","timestamp":1367997952000},"page":"3328-3339","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":82,"title":["Novel glyoxalases from <i><scp>A<\/scp>rabidopsis\u00a0thaliana<\/i>"],"prefix":"10.1111","volume":"280","author":[{"given":"Kyu","family":"Kwon","sequence":"first","affiliation":[{"name":"Department of Biological Sciences Korea Advanced Institute of Science and Technology Yuseong\u2010gu Daejeon Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dongwook","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Korea Advanced Institute of Science and Technology Yuseong\u2010gu Daejeon Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jae Kyung","family":"Hyun","sequence":"additional","affiliation":[{"name":"Division of Electron Microscopic Research Korea Basic Science Institute Daejeon Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyun Suk","family":"Jung","sequence":"additional","affiliation":[{"name":"Division of Electron Microscopic Research Korea Basic Science Institute Daejeon Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kwanghee","family":"Baek","sequence":"additional","affiliation":[{"name":"Department of Genetic Engineering and Graduate School of Biotechnology Kyung Hee University Yongin Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chankyu","family":"Park","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Korea Advanced Institute of Science and Technology Yuseong\u2010gu Daejeon 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