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Bst polymerase — a humble relative of Taq polymerase Научная публикация

Журнал Computational and Structural Biotechnology Journal
ISSN: 2001-0370
Вых. Данные Год: 2023, Том: 21, Страницы: 4519-4535 Страниц : 17 DOI: 10.1016/j.csbj.2023.09.008
Ключевые слова Bst polymeraseDNA polymeraseProcessivityFidelityStrand displacementSite-directed mutagenesisDirected evolutionFusion proteins
Авторы Oskorbin I.P. 1 , Filipenko M.L. 1
Организации
1 Laboratory of Pharmacogenomics, Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences (ICBFM SB RAS), 8 Lavrentiev Avenue, Novosibirsk 630090, Russia

Информация о финансировании (1)

1 МИНИСТЕРСТВО НАУКИ И ВЫСШЕГО ОБРАЗОВАНИЯ РОССИЙСКОЙ ФЕДЕРАЦИИ ПФНИ РФ (2021-2030) 0245-2021-0002

Реферат: DNA polymerases are a superfamily of enzymes synthesizing DNA using DNA as a template. They are essential for nucleic acid metabolism and for DNA replication and repair. Modern biotechnology and molecular diagnostics rely heavily on DNA polymerases in analyzing nucleic acids. Among a variety of discovered DNA polymerases, Bst polymerase, a large fragment of DNA polymerase I from Geobacillus stearothermophilus, is one of the most commonly used but is not as well studied as Taq polymerase. The ability of Bst polymerase to displace an upstream DNA strand during synthesis, coupled with its moderate thermal stability, has provided the basis for several isothermal DNA amplification methods, including LAMP, WGA, RCA, and many others. Bst polymerase is one of the key components defining the robustness and analytical characteristics of diagnostic test systems based on isothermal amplification. Here, we present an overview of the biochemical and structural features of Bst polymerase and provide information on its mutated analogs.
Библиографическая ссылка: Oskorbin I.P. , Filipenko M.L.
Bst polymerase — a humble relative of Taq polymerase
Computational and Structural Biotechnology Journal. 2023. V.21. P.4519-4535. DOI: 10.1016/j.csbj.2023.09.008 WOS Scopus PMID OpenAlex
Идентификаторы БД:
Web of science: WOS:001082229600001
Scopus: 2-s2.0-85172388627
PMID (PubMed): 37767105
OpenAlex: W4386629834
Цитирование в БД:
БД Цитирований
OpenAlex 29
Scopus 8
Web of science 18
Альметрики: