Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=FAD<.>)

Общее количество найденных документов : 4
Показаны документы с 1 по 4

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya, Olga, Ronzhin, Nikita, Posokhina, Ekaterina, Bondar, Vladimir
Заглавие : Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications
Колич.характеристики :10 с
Коллективы : [0356-2019-0022]
Место публикации : Protein J.: SPRINGER, 2021. - Article in press. - ISSN 1572-3887, DOI 10.1007/s10930-021-10010-z. - ISSN 1573-4943(eISSN)
Примечания : Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, Project No. 0356-2019-0022.
Предметные рубрики: ARYL-ALCOHOL OXIDASE
GLUCOSE-OXIDASE
PEROXIDASES
MECHANISM
Аннотация: The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with beta-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H2O2, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55-70 degrees C and pH 5.0. Kinetic parameters K-m and V-max of the oxidase for phenol were 0.21 mM and 0.40 mu M min(-1). We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.
WOS
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ronzhin N. O., Mogilnaya O. A., Artemenko K. S., Posokhina E. D., Bondar V. S.
Заглавие : Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties
Колич.характеристики :5 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2020. - Vol. 490, Is. 1. - С. 38-42. - ISSN 1607-6729, DOI 10.1134/S1607672920010135. - ISSN 1608-3091(eISSN)
Примечания : Cited References:15
Предметные рубрики: PEROXIDASE-ACTIVITY
LIGHT-EMISSION
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.
WOS
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deeva, Anna A., Zykova, Evgenia A., Nemtseva, Elena V., Kratasyuk, Valentina A.
Заглавие : Functional divergence between evolutionary-related LuxG and Fre oxidoreductases of luminous bacteria
Колич.характеристики :7 с
Коллективы : Russian Foundation for Basic Research [18-44-243009]; Ministry of Education and Science of the Russian Federation [0356-2019-0019, 6.7734.2017]; Krasnoyarsk Region Science and Technology [18-44-243009]
Место публикации : Proteins: WILEY, 2019. - Vol. 87, Is. 9. - С. 723-729. - ISSN 0887-3585, DOI 10.1002/prot.25696. - ISSN 1097-0134(eISSN)
Примечания : Cited References:39. - The Russian Foundation for Basic Research and Krasnoyarsk Region Science and Technology Support Fund, Grant/Award Number: 18-44-243009; Ministry of Education and Science of the Russian Federation, Grant/Award Numbers: 0356-2019-0019, 6.7734.2017
Предметные рубрики: ESCHERICHIA-COLI
FLAVIN OXIDOREDUCTASE
CRYSTAL-STRUCTURE
Аннотация: In luminous bacteria NAD(P)H:flavin-oxidoreductases LuxG and Fre, there are homologous enzymes that could provide a luciferase with reduced flavin. Although Fre functions as a housekeeping enzyme, LuxG appears to be a source of reduced flavin for bioluminescence as it is transcribed together with luciferase. This study is aimed at providing the basic conception of Fre and LuxG evolution and revealing the peculiarities of the active site structure resulted from a functional variation within the oxidoreductase family. A phylogenetic analysis has demonstrated that Fre and LuxG oxidoreductases have evolved separately after the gene duplication event, and consequently, they have acquired changes in the conservation of functionally related sites. Namely, different evolutionary rates have been observed at the site responsible for specificity to flavin substrate (Arg 46). Also, Tyr 72 forming a part of a mobile loop involved in FAD binding has been found to be conserved among Fre in contrast to LuxG oxidoreductases. The conservation of different amino acid types in NAD(P)H binding site has been defined for Fre (arginine) and LuxG (proline) oxidoreductases.
WOS,
Смотреть статью
Найти похожие

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Lee J.
Заглавие : Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1
Место публикации : European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - С. 790-796. - ISSN 00142956 (ISSN)
Ключевые слова (''Своб.индексиров.''): anisotropy--lumazine protein--photobacterium--thioredoxin reductase--time-resolved fluorescence--cytochrome--flavoprotein--article--bioluminescence--nonhuman--priority journal--protein analysis--protein purification--sea--vibrio--amino acid sequence--bacterial proteins--cytochromes--flavoproteins--molecular sequence data--sequence alignment--vibrio--azotobacter--bacteria (microorganisms)--escherichia coli--haemophilus--haemophilus influenza--murinae--negibacteria--photobacterium--photobacterium leiognathi--pseudomonas--uncultured marine bacterium--vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.
Scopus
Найти похожие

Тематический навигатор

Другие библиотеки

Библиотека института физики

Центральная научная библиотека КНЦ СО РАН

Библиотека института химии и химический технологии

Библиотека института вычислительного моделирования

Библиотека института леса

Библиотека СФУ

Краевая научная библиотека

© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)