17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus:: structural and functional aspects

被引：18
作者：
Rizner, TL
Stojan, J
Adamski, J
机构：
[1] Univ Ljubljana, Fac Med, Inst Biochem, Ljubljana 1000, Slovenia
[2] GSF, Natl Res Ctr Environm & Hlth, Inst Expt Genet, Neuherberg, Germany
来源：
CHEMICO-BIOLOGICAL INTERACTIONS | 2001年 / 130卷 / 1-3期
关键词：
17 beta-hydroxysteroid dehydrogenase; short chain dehydrogenases/reductases; fungi; Cochliobolus lunatus;
D O I：
10.1016/S0009-2797(00)00235-0
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
17 beta -Hydroxysteroid debydrogenase (17 beta -HSD) activity has been described in all filamentous fungi tested, but until now only one 17 beta -HSD from Cochliobolus lunatus (17 beta -HSDcl) was sequenced. We examined the evolutionary relationship among 17 beta -HSDcl, fungal reductases, versicolorin reductase (Ver1), trihydroxynaphthalene reductase (THNR), and other homologous proteins. In the phylogenetic tree 17 beta -HSDcl formed a separate branch with Veri, while THNRs reside in another branch, indicating that 17 beta -HSDcl could have similar function as Veri. The structural relationship was investigated by comparing a model structure of 17P-HSDcl to several known crystal structures of the short chain dehydrogenase/reductase (SDR) family. A similarity was observed to structures of bacterial 7 alpha -HSD and plant tropinone reductase (TR). Additionally, substrate specificity revealed that among the substrates tested the 17 beta -HSDcl preferentially catalyzed reductions of steroid substrates with a 3-keto group, Delta (4) or 5 alpha such as: 4-estrene-3,17-dione and 5 alpha -androstane-3,17-dione. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
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页码：793 / 803
页数：11
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