Supramolecular Organization of Inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus: A Comparative Aspect
- Autores: Holyavka M.G.1, Makin S.M.1, Kondratyev M.S.2, Abdullatypov A.V.3, Kovaleva T.A.1, Artyukhov V.G.1
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Afiliações:
- Voronezh State University
- Institute of Cell Biophysics, Russian Academy of Sciences
- Institute of Basic Biological Problems, Russian Academy of Sciences
- Edição: Volume 63, Nº 6 (2018)
- Páginas: 866-875
- Seção: Molecular Biophysics
- URL: https://ogarev-online.ru/0006-3509/article/view/152776
- DOI: https://doi.org/10.1134/S0006350918060155
- ID: 152776
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Resumo
Computer models for the dimers of inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus have been developed. The inulinases dimerization mechanisms from various producers and the amino acid composition of binding sites between the monomers in dimer structure have been studied. Exoinulinase dimers are more similar in structure than endoinulinase dimer. Nonpolar amino acids play the key role in the process of inulinase dimerization during the formation of a bond between the monomer forms of the enzyme from both molds and yeast.
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Sobre autores
M. Holyavka
Voronezh State University
Autor responsável pela correspondência
Email: holyavka@rambler.ru
Rússia, Voronezh, 394018
S. Makin
Voronezh State University
Email: azatik888@yandex.ru
Rússia, Voronezh, 394018
M. Kondratyev
Institute of Cell Biophysics, Russian Academy of Sciences
Autor responsável pela correspondência
Email: ma-ko@bk.ru
Rússia, Pushchino, Moscow oblast, 142290
A. Abdullatypov
Institute of Basic Biological Problems, Russian Academy of Sciences
Autor responsável pela correspondência
Email: azatik888@yandex.ru
Rússia, Pushchino, Moscow oblast, 142290
T. Kovaleva
Voronezh State University
Email: azatik888@yandex.ru
Rússia, Voronezh, 394018
V. Artyukhov
Voronezh State University
Email: azatik888@yandex.ru
Rússia, Voronezh, 394018
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