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One of the most promising methods to detoxify this mycotoxin involves its enzymatic epimerization to 3-\n                    <jats:italic>epi<\/jats:italic>\n                    -DON. DepB plays a critical role in this process by reducing 3-keto-DON, an intermediate in the epimerization process, to 3-\n                    <jats:italic>epi<\/jats:italic>\n                    -DON. DepB\n                    <jats:sub>Rleg<\/jats:sub>\n                    from\n                    <jats:italic>Rhizobium leguminosarum<\/jats:italic>\n                    is a member of the new aldo\u2013keto reductase family, AKR18, and it has the unusual ability to utilize both NADH and NADPH as coenzymes, albeit with a 40-fold higher catalytic efficiency with NADPH compared to NADH. Structural analysis of DepB\n                    <jats:sub>Rleg<\/jats:sub>\n                    revealed the putative roles of Lys-217, Arg-290, and Gln-294 in NADPH specificity. Replacement of these residues by site-specific mutagenesis to negatively charged amino acids compromised NADPH binding with minimal effects on NADH binding. The substrate-binding site of DepB\n                    <jats:sub>Rleg<\/jats:sub>\n                    is larger than its closest structural homolog, AKR6A2, likely contributing to its ability to utilize a wide range of aldehydes and ketones, including the mycotoxin, patulin, as substrates. The structure of DepB\n                    <jats:sub>Rleg<\/jats:sub>\n                    also suggests that 3-keto-DON can adopt two binding modes to facilitate 4-\n                    <jats:italic>pro<\/jats:italic>\n                    -R hydride transfer to either the\n                    <jats:italic>re<\/jats:italic>\n                    - or\n                    <jats:italic>si<\/jats:italic>\n                    -face of the C3 ketone providing a possible explanation for the enzyme\u2019s ability to convert 3-keto-DON to 3-\n                    <jats:italic>epi<\/jats:italic>\n                    -DON and DON in diastereomeric ratios of 67.2% and 32.8% respectively.\n                  <\/jats:p>","DOI":"10.1038\/s41598-022-19040-8","type":"journal-article","created":{"date-parts":[[2022,8,30]],"date-time":"2022-08-30T06:02:32Z","timestamp":1661839352000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":45,"title":["Structure\u2013function characterization of an aldo\u2013keto reductase involved in detoxification of the mycotoxin, deoxynivalenol"],"prefix":"10.1038","volume":"12","author":[{"given":"Nadine","family":"Abraham","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kurt L.","family":"Schroeter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan","family":"Chan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natasha","family":"Evans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew S.","family":"Kimber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jason","family":"Carere","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ting","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen Y. 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