Conformational stability of 17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus
نویسندگان
چکیده
منابع مشابه
A novel 17beta-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: new insights into the evolution of steroid-hormone signalling.
17beta-Hydroxysteroid dehydrogenase (17beta-HSD) from the filamentous fungus Cochliobolus lunatus (17beta-HSDcl) catalyses the reduction of steroids and of several o- and p-quinones. After purification of the enzyme, its partial amino acid sequence was determined. A PCR fragment amplified with primers derived from peptide sequences was generated for screening the Coch. lunatus cDNA library. Thr...
متن کاملBiotransformation of Digitoxigenin by Cochliobolus lunatus
A reação de biotransformação da digitoxigenina (1) por Cochliobolus lunatus foi investigada. Foram realizados experimentos com duração de 4 dias, que resultaram no isolamento de quatro produtos, cujas estruturas químicas foram elucidadas como sendo 1β-hidroxidigitoxigenina (2), 7β-hidroxidigitoxigenina (3), 8β-hidroxidigitoxigenina (4) e digitoxigenona (5). A obtenção desses produtos nas condiç...
متن کاملExpression patterns of 17β-hydroxysteroid dehydrogenase 14 in human tissues.
17βHSD enzymes catalyze the stereospecific oxidation/reduction at carbon 17β of androgens and estrogens, and are important players in intracrine sex hormone synthesis. The biological relevance of 17βHSD14, first named retSDR3, is largely unknown. We generated and validated an antibody targeting the 17βHSD14 antigen and used this for immunohistochemical evaluation of expression patterns in 33 he...
متن کاملRoles of 17β-hydroxysteroid dehydrogenase type 10 in neurodegenerative disorders
17β-Hydroxysteroid dehydrogenase type 10 (17β-HSD10) is encoded by the HSD17B10 gene mapping at Xp11.2. This homotetrameric mitochondrial multifunctional enzyme catalyzes the oxidation of neuroactive steroids and the degradation of isoleucine. This enzyme is capable of binding to other peptides, such as estrogen receptor α, amyloid-β, and tRNA methyltransferase 10C. Missense mutations of the HS...
متن کاملInsights into subtle conformational differences in the substrate-binding loop of fungal 17β-hydroxysteroid dehydrogenase: a combined structural and kinetic approach.
The 17β-HSD (17β-hydroxysteroid dehydrogenase) from the filamentous fungus Cochliobolus lunatus (17β-HSDcl) is a NADP(H)-dependent enzyme that preferentially catalyses the interconversion of inactive 17-oxo-steroids and their active 17β-hydroxy counterparts. 17β-HSDcl belongs to the SDR (short-chain dehydrogenase/reductase) superfamily. It is currently the only fungal 17β-HSD member that has be...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Journal
سال: 2006
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2006.05396.x