Avtor/Urednik | Lanišnik-Rižner, T; Stojan, J; Adamski, J | |
Naslov | 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: structural and functional aspects | |
Tip | članek | |
Vir | Chem Biol Interact | |
Vol. in št. | Letnik 130-2, št. 1-3 | |
Leto izdaje | 2001 | |
Obseg | str. 793-803 | |
Jezik | eng | |
Abstrakt | 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 homologous proteins. 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, such as: 4-estrene-3,17-dione and 5alpha-androstane-3,17-dione. | |
Deskriptorji | 17-HYDROXYSTEROID DEHYDROGENASES ASCOMYCETES MODELS, MOLECULAR PHYLOGENY PROTEIN CONFORMATION SUBSTRATE SPECIFICITY |