{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T12:06:53Z","timestamp":1788264413115,"version":"build-2803163510"},"reference-count":36,"publisher":"Wiley","issue":"20","license":[{"start":{"date-parts":[[2015,8,14]],"date-time":"2015-08-14T00:00:00Z","timestamp":1439510400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Tokai University Educational System"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2015,10]]},"abstract":"<jats:p>A gene encoding a functionally unknown protein that is specifically expressed in the thyroidectomized chicken fatty liver and has a predicted amino acid sequence similar to that of <jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content>(P)H\u2010dependent carbonyl reductase was overexpressed in <jats:italic>Escherichia\u00a0coli<\/jats:italic>; its product was purified and characterized. The expressed enzyme was an <jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content>(P)H\u2010dependent broad substrate specificity carbonyl reductase and was inhibited by arachidonic acid at 1.5\u00a0\u03bc<jats:sc>m<\/jats:sc>. Enzymological characterization indicated that the enzyme could be classified as a cytosolic\u2010type carbonyl reductase. The enzyme's 3D structure was determined using the molecular replacement method at 1.98\u00a0\u00c5 resolution in the presence of <jats:styled-content style=\"fixed-case\">NADPH<\/jats:styled-content> and ethylene glycol. The asymmetric unit consisted of two subunits, and a noncrystallographic twofold axis generated the functional dimer. The structures of the subunits, A and B, differed from each other. In subunit\u00a0A, the active site contained an ethylene glycol molecule absent in subunit\u00a0B. Consequently, Tyr172 in subunit\u00a0A rotated by 103.7\u00b0 in comparison with subunit\u00a0B, which leads to active site closure in subunit\u00a0A. In Y172A mutant, the <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> value for 9,10\u2010phenanthrenequinone (model substrate) was 12.5\u00a0times higher than that for the wild\u2010type enzyme, indicating that Tyr172 plays a key role in substrate binding in this carbonyl reductase. Because the Tyr172\u2010containing active site lid structure (Ile164\u2013Gln174) is not conserved in all known carbonyl reductases, our results provide new insights into substrate binding of carbonyl reductase. The catalytic properties and crystal structure revealed that thyroidectomized chicken fatty liver carbonyl reductase is a novel enzyme.<\/jats:p>","DOI":"10.1111\/febs.13385","type":"journal-article","created":{"date-parts":[[2015,7,23]],"date-time":"2015-07-23T14:04:48Z","timestamp":1437660288000},"page":"3918-3928","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["A novel <scp>NAD<\/scp>(P)H\u2010dependent carbonyl reductase specifically expressed in the thyroidectomized chicken fatty liver: catalytic properties and crystal structure"],"prefix":"10.1111","volume":"282","author":[{"given":"Yudai","family":"Fukuda","sequence":"first","affiliation":[{"name":"Department of Bioscience Tokai University Kumamoto Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takeki","family":"Sone","sequence":"additional","affiliation":[{"name":"Department of Bioscience Tokai University Kumamoto 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