vavilovВавиловский журнал генетики и селекцииVavilov Journal of Genetics and Breeding2500-3259Institute of Cytology and Genetics of Siberian Branch of the RASvavilov-191Research ArticleСтатьиArticlesКОМПЬЮТЕРНЫЙ АНАЛИЗ СТРУКТУРЫ ЛИПАЗ БАКТЕРИЙ pода Geobacillus И ВЫЯВЛЕНИЕ МОТИВОВ, ВЛИЯЮЩИХ НА ИХ ТЕРМОСТАБИЛЬНОСТЬCOMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITYСорокинаК. Н.SorokinaK. N.k.sorokina@gmail.comНуриддиновМ. А.NuriddinovM. A.k.sorokina@gmail.comРозановА. С.RozanovA. S.k.sorokina@gmail.comИванисенкоВ. А.IvanisenkoV. A.k.sorokina@gmail.comПельтекС. Е.PeltekS. E.k.sorokina@gmail.comФедеральное государственное бюджетное научное учреждение «Федеральный исследовательский центр Институт цитологии и генетики Сибирского отделения Российской академии наук», Новосибирск, РоссияРоссияInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaRussian Federation201310012015174/1666674Copyright © Сорокина К.Н., Нуриддинов М.А., Розанов А.С., Иванисенко В.А., Пельтек С.Е., 20152015Сорокина К.Н., Нуриддинов М.А., Розанов А.С., Иванисенко В.А., Пельтек С.Е.Sorokina K.N., Nuriddinov M.A., Rozanov A.S., Ivanisenko V.A., Peltek S.E.This work is licensed under a Creative Commons Attribution 4.0 License.https://vavilov.elpub.ru/jour/article/view/191

В работе проведен анализ свойств термостабильных липаз бактерий рода Geobacillus. Проведена классификация ферментов по группам термостабильности. Показано наличие согласованных аминокислотных замен у группы липаз с высокой термостабильностью (со временем полуинактивации свыше 1000 мин): V198A, Q203E, V204I, Q217E и V294I, P306A, T307A, D312S, R313H, E316G, V324I, S334N, A343T. Наибольшее достоверное влияние на термостабильность ферментов оказывал гидрофильный момент α-спиралей, который коррелировал с зарядом и полярностью аминокислотных остатков данных регионов. Показано, что у липаз с наибольшей термостабильностью происходит стабилизация «lid»-домена на структурном уровне в районе 198А-217Е.

Properties of thermostable lipases from Geobacillus bacteria are considered. The enzymes are divided into groups with regard to their thermostability. Coordinated amino acid substitutions are demonstrated in the highly thermostable group (half-inactivation time > 1000 min); V198A, Q203E, V204I, Q217E; and V294I, P306A, T307A, D312S, R313H, E316G, V324I, S334N, A343T. The hydrophilic moment of α helices, correlating with the charge and polarity of amino acid in the region, exerts the most significant influence on enzyme thermostability. Most thermostable lipases are characterized by structural stabilization of the lid domain in the 198А-217Е region.

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The authors declare that there are no conflicts of interest present.