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Structuraldistinctions of fastand slow bacterialluciferases revealedby phylogeneticanalysis Deeva Anna A.Temlyakova Evgenia A.Sorokin Anatoly A.2016 год

Structural distinctions of fast and slow bacterial luciferases revealed by phylogenetic analysis
статья из журнала

Дополнительные ссылки: WOS · Scopus · eLibrary
База данных: Каталог библиотеки СФУ
Библиографическое описание: Structural distinctions of fast and slow bacterial luciferases revealed by phylogenetic analysis / A. A. Deeva [et al.]. - Текст : непосредственный // Bioinformatics. - 2016. - Vol. 32, Is. 20. - P. 3053-3057. - Cited Reference Count: 31. - Гранты: The reported study was partially funded by RFBR according to the research project No. 16-34-00746 mol_a; by the Ministry of Education and Science of the Russian Federation [project No 1762] and by the state budget allocated to the fundamental research at the Russian Academy of Sciences [project No 01201351504]. - Финансирующая организация: RFBR [16-34-00746 mol_a]; Ministry of Education and Science of the Russian Federation [1762]; state budget allocated to the fundamental research at Russian Academy of Sciences [01201351504]. - OCT 15. - ISSN 1367-4803. - ISSN 1460-2059, DOI 10.1093/bioinformatics/btw386.
Аннотация: Motivation: Bacterial luciferases are heterodimeric enzymes that catalyze a chemical reaction, so called bioluminescence, which causes light emission in bacteria. Bioluminescence is vastly used as a reporter system in research tools and commercial developments. However, the details of the mechanisms that stabilize and transform the reaction intermediates as well as differences in the enzymatic kinetics amongst different bacterial luciferases remain to be elucidated. Results: Amino acid sequences alignments for 21 bacterial luciferases (both alpha- and beta-subunits) were analyzed. For alpha-subunit, containing the enzyme active center, 48 polymorphic amino acid positions were identified. According to them, the sequences fell into two distinct groups known as slow and fast based on the decay rate of the bioluminescence reaction. The differences in the enzyme active site induced by structural polymorphism are analyzed.
Год издания: 2016
Авторы: Deeva Anna A. , Temlyakova Evgenia A. , Sorokin Anatoly A. , Nemtseva Elena V. , Kratasyuk Valentina A.
Издательство: OXFORD UNIV PRESS, OXFORD
Источник: BIOINFORMATICS
Выпуск: Vol. 32, Is. 20
Номера страниц: 3053-3057
Держатель оригинала документа: Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia, Inst Cell Biophys RAS, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia, Moscow Inst Phys & Technol, Dolgoprudnyi, Russia, Inst Biophys SB RAS, Lab Photobiol, Krasnoyarsk, Russia
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