{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,25]],"date-time":"2025-10-25T11:54:47Z","timestamp":1761393287616},"reference-count":47,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,5]],"date-time":"2005-02-05T00:00:00Z","timestamp":1107561600000},"content-version":"vor","delay-in-days":3323,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["BioEssays"],"published-print":{"date-parts":[[1996,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>11\u03b2\u2010hydroxysteroid dehydrogenases regulate glucocorticoid concentrations and 17\u03b2\u2010hydroxysteroid dehydrogenases regulate estrogen and androgen concentrations in mammals. Phylogenetic analysis of the sequences from two 11\u03b2\u2010hydroxysteroid dehydrogenases and four mammalian 17\u03b2\u2010hydroxysteroid dehydrogenases indicates unusual evolution in these enzymes. Type 1 11\u03b2\u2010 and 17\u03b2\u2010hydroxysteroid dehydrogenases are on the same branch; Type 2 enzymes cluster on another branch with \u03b2\u2010hydroxybutyrate dehydrogenase, 11\u2010<jats:italic>cis<\/jats:italic> retinol dehydrogenase and retinol dehydrogenase; Type 3 17\u03b2\u2010hydroxysteroid dehydrogenase is on a third branch; while the pig dehydrogenase clusters with a yeast multifunctional enzyme on a fourth branch. Pig 17\u03b2\u2010hydroxysteroid dehydrogenase appears to have evolved independently from the other three 17\u03b2\u2010hydroxysteroid dehydrogenase dehydrogenases; in which case, the evolution of 17\u03b2\u2010hydroxysteroid dehydrogenase activity is an example of functional convergence. The phylogeny also suggests that independent evolution of specificity toward C11 substituents on glucocorticoids and C17 substituents on androgens and estrogens has occurred in Types 1 and 2 11\u03b2\u2010 and 17\u03b2\u2010hydroxysteroid dehydrogenases.<\/jats:p>","DOI":"10.1002\/bies.950180112","type":"journal-article","created":{"date-parts":[[2005,2,25]],"date-time":"2005-02-25T07:36:37Z","timestamp":1109316997000},"page":"63-70","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Unusual evolution of 11\u03b2\u2010 and 17\u03b2\u2010hydroxysteroid and retinol dehydrogenases"],"prefix":"10.1002","volume":"18","author":[{"given":"Michael E.","family":"Baker","sequence":"first","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,5]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1992.tb17310.x"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1210\/mend-3-5-881"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0039-128X(91)90067-6"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1991.tb16215.x"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0303-7207(92)90064-D"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.250.4983.948"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/357655a0"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3000605b"},{"key":"e_1_2_1_10_2","first-page":"16653","article-title":"The human gene for 11\u03b2\u2010hydroxysteroid dehydrogenase","volume":"266","author":"Tannin G. 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