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Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties. / Bulygin, A. A.; Kuznetsova, A. A.; Fedorova, O. S. et al.

In: Molecular Biology, Vol. 57, No. 2, 04.2023, p. 182-192.

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Bulygin AA, Kuznetsova AA, Fedorova OS, Kuznetsov NA. Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties. Molecular Biology. 2023 Apr;57(2):182-192. doi: 10.1134/S0026893323020048

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Bulygin, A. A. ; Kuznetsova, A. A. ; Fedorova, O. S. et al. / Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties. In: Molecular Biology. 2023 ; Vol. 57, No. 2. pp. 182-192.

BibTeX

@article{3ea3e3de9f17429b907f8122564befd4,
title = "Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties",
abstract = "DNA polymerases catalyze DNA synthesis during DNA replication, repair, and recombination. A number of DNA polymerases, such as the Taq enzyme from Thermus aquaticus, are used in various applications of molecular biology and biotechnology, in particular as DNA amplification tools. However, the efficiency of these enzymes depends on factors such as DNA origin, primer composition, template length, GC-content, and the ability to form stable secondary structures. These limitations in the use of currently known DNA polymerases lead to the search for new enzymes with improved properties. This review summarizes the main structural and molecular-kinetic features of the functioning of DNA-polymerases belonging to structural family A, including Taq polymerase. A phylogenetic analysis of these enzymes was carried out, which made it possible to establish a highly conserved consensus sequence containing 62 amino acid residues distributed over the structure of the enzyme. A comparative analysis of these amino acid residues among poorly studied DNA-polymerases revealed 7 enzymes that potentially have the properties necessary for use in DNA amplification.",
keywords = "DNA-polymerase, active site, catalytic mechanism, kinetics, protein-nucleic acid interactions, structural family",
author = "Bulygin, {A. A.} and Kuznetsova, {A. A.} and Fedorova, {O. S.} and Kuznetsov, {N. A.}",
note = "The work was supported by the Ministry of Science and Higher Education, agreement no. 075-15-2021-1085. Публикация для корректировки.",
year = "2023",
month = apr,
doi = "10.1134/S0026893323020048",
language = "English",
volume = "57",
pages = "182--192",
journal = "Molecular Biology",
issn = "0026-8933",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "2",

}

RIS

TY - JOUR

T1 - Comparative Analysis of Family A DNA-Polymerases as a Searching Tool for Enzymes with New Properties

AU - Bulygin, A. A.

AU - Kuznetsova, A. A.

AU - Fedorova, O. S.

AU - Kuznetsov, N. A.

N1 - The work was supported by the Ministry of Science and Higher Education, agreement no. 075-15-2021-1085. Публикация для корректировки.

PY - 2023/4

Y1 - 2023/4

N2 - DNA polymerases catalyze DNA synthesis during DNA replication, repair, and recombination. A number of DNA polymerases, such as the Taq enzyme from Thermus aquaticus, are used in various applications of molecular biology and biotechnology, in particular as DNA amplification tools. However, the efficiency of these enzymes depends on factors such as DNA origin, primer composition, template length, GC-content, and the ability to form stable secondary structures. These limitations in the use of currently known DNA polymerases lead to the search for new enzymes with improved properties. This review summarizes the main structural and molecular-kinetic features of the functioning of DNA-polymerases belonging to structural family A, including Taq polymerase. A phylogenetic analysis of these enzymes was carried out, which made it possible to establish a highly conserved consensus sequence containing 62 amino acid residues distributed over the structure of the enzyme. A comparative analysis of these amino acid residues among poorly studied DNA-polymerases revealed 7 enzymes that potentially have the properties necessary for use in DNA amplification.

AB - DNA polymerases catalyze DNA synthesis during DNA replication, repair, and recombination. A number of DNA polymerases, such as the Taq enzyme from Thermus aquaticus, are used in various applications of molecular biology and biotechnology, in particular as DNA amplification tools. However, the efficiency of these enzymes depends on factors such as DNA origin, primer composition, template length, GC-content, and the ability to form stable secondary structures. These limitations in the use of currently known DNA polymerases lead to the search for new enzymes with improved properties. This review summarizes the main structural and molecular-kinetic features of the functioning of DNA-polymerases belonging to structural family A, including Taq polymerase. A phylogenetic analysis of these enzymes was carried out, which made it possible to establish a highly conserved consensus sequence containing 62 amino acid residues distributed over the structure of the enzyme. A comparative analysis of these amino acid residues among poorly studied DNA-polymerases revealed 7 enzymes that potentially have the properties necessary for use in DNA amplification.

KW - DNA-polymerase

KW - active site

KW - catalytic mechanism

KW - kinetics

KW - protein-nucleic acid interactions

KW - structural family

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85156109967&origin=inward&txGid=902a8ff0fa75bbc648ba96cf3ecca07c

UR - https://www.mendeley.com/catalogue/150d15ec-52ee-3ed4-8c45-176ecb67880e/

U2 - 10.1134/S0026893323020048

DO - 10.1134/S0026893323020048

M3 - Article

VL - 57

SP - 182

EP - 192

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 59649353