{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T17:04:19Z","timestamp":1770483859294,"version":"3.49.0"},"reference-count":40,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":3744,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1998,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The three\u2010dimensional structure of betaine aldehyde dehydrogenase, the most abundant aldehyde dehydrogenase (ALDH) of cod liver, has been determined at 2.1 \u00c5 resolution by the X\u2010ray crysallographic method of molecular replacement. This enzyme represents a novel structure of the highly multiple ALDH, with at least 12 distinct classes in humans. This betaine ALDH of class 9 is different from the two recently determined ALDH structures (classes 2 and 3). Like these, the betaine ALDH structure has three domains, one coenzyme binding domain, one catalytic domain, and one oligomerization domain. Crystals grown in the presence or absence of NAD<jats:sup>+<\/jats:sup> have very similar structures and no significant conformational change occurs upon coenzyme binding. This is probably due to the tight interactions between domains within the subunit and between subunits in the tetramer. The oligomerization domains link the catalytic domains together into two 20\u2010stranded pleated sheet structures. The overall structure is similar to that of the tetrameric bovine class 2 and dimeric rat class 3 ALDH, but the coenzyme binding with the nicotinamide in <jats:italic>anti<\/jats:italic> conformation, resembles that of class 2 rather than of class 3.<\/jats:p>","DOI":"10.1002\/pro.5560071007","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T06:14:14Z","timestamp":1234246454000},"page":"2106-2117","source":"Crossref","is-referenced-by-count":117,"title":["Structure of betaine aldehyde dehydrogenase at 2.1 \u00c5 resolution"],"prefix":"10.1002","volume":"7","author":[{"given":"Kenth","family":"Johansson","sequence":"first","affiliation":[]},{"given":"S.","family":"Ramaswamy","sequence":"additional","affiliation":[]},{"given":"Hans","family":"Eklund","sequence":"additional","affiliation":[]},{"given":"Mustapha","family":"El\u2010Ahmad","sequence":"additional","affiliation":[]},{"given":"Lars","family":"Hjelmqvist","sequence":"additional","affiliation":[]},{"given":"Hans","family":"J\u00f6rnvall","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0263-7855(98)80030-1"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/6.1.37"},{"key":"e_1_2_1_3_2","first-page":"760","article-title":"The CCP4 suite: Programs for protein crystallography","volume":"50","author":"CCP4","year":"1994","journal-title":"Acta Cryst"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1995.2168"},{"key":"e_1_2_1_5_1","first-page":"34","article-title":"DM. 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