دورية أكاديمية
Physical and chemical properties of Δ3−12 cysteine-depleted cytocrome P450 3A4 with amino acid substitution of S291C ; Физико-химические свойства Δ3−12 цистеин-обедненного цитохрома P450 3A4 с аминокислотной заменой S291C
| العنوان: | Physical and chemical properties of Δ3−12 cysteine-depleted cytocrome P450 3A4 with amino acid substitution of S291C ; Физико-химические свойства Δ3−12 цистеин-обедненного цитохрома P450 3A4 с аминокислотной заменой S291C |
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| المؤلفون: | V. V. Britikov, E. V. Britikova, E. V. Bocharov, Ya. V. Bershatsky, N. V. Kuzmina, K. M. Boyko, S. A. Usanov, В. В. Бритиков, Е. В. Бритикова, Э. В. Бочаров, Я. В. Бершацкий, Н. В. Кузьмина, К. М. Бойко, С. А. Усанов |
| المساهمون: | The research is financially sponsored by the Belarusian Republican Foundation of Fundamental Research and the Russian Foundation of Basic Research (Projects No. Х20Р-159 and No. 20-54-00041Бел_а), Работа была выполнена при финансовой поддержке БРФФИ и РФФИ (проекты № Х20Р-159 и № 20-54-00041Бел_а) |
| المصدر: | Doklady of the National Academy of Sciences of Belarus; Том 66, № 2 (2022); 176-186 ; Доклады Национальной академии наук Беларуси; Том 66, № 2 (2022); 176-186 ; 2524-2431 ; 1561-8323 ; 10.29235/1561-8323-2022-66-2 |
| بيانات النشر: | The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka" |
| سنة النشر: | 2022 |
| المجموعة: | Doklady of the National Academy of Sciences of Belarus (E-Journal) / Доклады Национальной академии наук Беларуси |
| مصطلحات موضوعية: | спектроскопия кругового дихроизма, human microsomal cytochrome b5, protein engineering, site-directed mutagenesis, hydroxylase activity, circular dichroism spectroscopy, микросомальный цитохром b5 человека, белковая инженерия, сайт-направленный мутагенез, гидроксилазная активность |
| الوصف: | Cytochrome P450 3A4 (3A4) is highly expressed in the human liver cells and plays a decisive role in the metabolism of xenobiotics, including more than 50 % of medical products. The activity of this enzyme can be regulated at the expression level of genes, as well as at the conformation level of the structure of the protein itself, due to changes in the molecular environment, including due to the interaction with high-molecular effectors. The understanding of the structure changes and the 3A4 dynamics in response to the environmental changes is necessary to predict the changes in the level of its activity that to a considerable extent regulates the body’s homeostasis. To perform in vitro experiments on the structure, dynamics, and protein-ligand/protein interactions of the enzymes by the modern spectral methods, the approach is used, in which the target protein is selectively added with cysteine residues in the given polypeptide chain loci by the protein engineering methods for subsequent labeling with specialized molecular labels. To do this, the human mutant form of membrane-bound (full length) recombinant cytochrome P450 3A4 C58A/C64M/C98A/C239T/C377A/C468S/S291C was obtained. According to the circular dichroism spectroscopy data we established that the introduced mutations do not cause significant changes in the secondary structure of the obtained form 3A4, which shows the preservation of the folding of the peptide chain. The spectral photometric measurements were made to comparatively analyze the changes in the affinity to the ligands of the active center. Moreover, we showed that the testosterone hydroxylase activity in the in vitro reconstructed system for a given mutation form of 3A4 increases many times with respect to the wild form of the enzyme. ; Цитохром P450 3A4 (3A4) экспрессируется в клетках печени человека и играет ключевую роль в метаболизме ксенобиотиков, в том числе и более 50 % лекарственных препаратов. Регуляция активности данного фермента может происходить на уровне экспрессии генов, а ... |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | Russian |
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| DOI: | 10.29235/1561-8323-2022-66-2-176-186 |
| الإتاحة: | https://doi.org/10.29235/1561-8323-2022-66-2-176-186Test https://doi.org/10.29235/1561-8323-2022-66-2Test https://doi.org/10.1074/jbc.c400293200Test https://doi.org/10.1073/pnas.0603236103Test https://doi.org/10.1021/bi4005396Test https://doi.org/10.1016/j.drudis.2014.03.012Test https://doi.org/10.1021/acs.biochem.5b00510Test https://doi.org/10.1016/j.jinorgbio.2018.03.002Test https://doi.org/10.1074/jbc.ra117.000961Test https://doi.org/10.1002/cbic.200600142Test |
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| رقم الانضمام: | edsbas.AA230A59 |
| قاعدة البيانات: | BASE |
| DOI: | 10.29235/1561-8323-2022-66-2-176-186 |
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