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  • 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: structural and functional aspects
    Lanišnik-Rižner, Tea ; Stojan, Jure, 1956- ; Adamski, Jerzy, molekularna biologija
    17beta-Hydroxysteroid dehydrogenase (17beta-HSD) activity has been described in all filamentous fungi tested, but until now only one 17beta-HSD from Cochliobolus lunatus (17beta-HSDcl) was sequenced. ... We examined the evolutionary relationship among 17beta-HSDcl, fungal reductases, versicolorin reductase (Ver1), trihydroxynaphthalene reductase (THNR), and other homologousproteins. In the phylogenetic tree 17beta-HSDcl formed a separate branch with Ver1, while THNRs reside in another branch, indicating that 17beta-HSDcl could have similar function as Ver1. The structural relationship was investigated by comparing a model structure of 17beta-HSDcl to several known crystal structures of the short chain dehydrogenase/reductase (SDR) family. A similarity was observed to structures of bacterial 7alpha-HSD and plant tropinone reductase (TR). Additionally, substrate specificity revealed that among the substrates tested the 17beta-HSDcl preferentially catalyzed reductions of steroid substrates with a 3-keto group, Delta(4) or 5alpha, suchas: 4-estrene-3,17-dione and 5alpha-androstane-3,17-dione.
    Vir: Chemico-biological interactions. - ISSN 0009-2797 (Letn. 130/2, št. 1/3, 2001, str. 793-803)
    Vrsta gradiva - članek, sestavni del
    Leto - 2001
    Jezik - angleški
    COBISS.SI-ID - 12915417
vir: Chemico-biological interactions. - ISSN 0009-2797 (Letn. 130/2, št. 1/3, 2001, str. 793-803)
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