Introduction of additional thiol groups into glucoamylase in Aspergillus Awamori and their effect on the thermal stability and catalytic activity of the enzyme. Surzhik, M., Schmidt, A., Glazunov, E., Firsov, D., & Petukhov, M. Applied Biochemistry and Microbiology, 50(2):118-124, 2014. cited By 3![Introduction of additional thiol groups into glucoamylase in Aspergillus Awamori and their effect on the thermal stability and catalytic activity of the enzyme [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Five mutant forms of glucoamylase (GA) from the filamentous fungus Aspergillus awamori with artificial disulfide bonds (4D-G137A\A14C, 6D-A14C\Y419C\G137A, 10D-V13C\G396C, 11D-V13C\G396C\A14C\Y419C\G137A, and 20D-G137A\A246C\A14C) were constructed using molecular modeling simulations and experimentally tested for thermostability. The introduction of two additional disulfide bonds between its first and thirteenth α-helices and that of the loop located close to a catalytic residue-E400-made it possible to assess the effects of disulfide bridges on protein thermostability. The mutant proteins with combined amino acid substitutions G137A\A14C, V13C\G396C\A14C\Y419C\G137A, and G137A\A246C\A14C showed higher thermal stability as compared to the wild-type protein. At the same time, new disulfide bridges in the mutant A14C\Y419C\G137A and V13C\G396C proteins led to the destabilization of their structure and the loss of thermal stability. © 2014 Pleiades Publishing, Inc.
@ARTICLE{Surzhik2014118,
author={Surzhik, M.A. and Schmidt, A.E. and Glazunov, E.A. and Firsov, D.L. and Petukhov, M.G.},
title={Introduction of additional thiol groups into glucoamylase in Aspergillus Awamori and their effect on the thermal stability and catalytic activity of the enzyme},
journal={Applied Biochemistry and Microbiology},
year={2014},
volume={50},
number={2},
pages={118-124},
doi={10.1134/S0003683814020185},
note={cited By 3},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84897790640&doi=10.1134%2fS0003683814020185&partnerID=40&md5=71e70330501a996dfb4ab4ef6c53ceda},
affiliation={Konstantinov Institute of Nuclear Physics, National Research Centre Kurchatov Institute, Gatchina, Leningrad oblast, 188300, Russian Federation; Department of Biophysics, Institute of Physics, Nanotechnology, and Telecommunications, St. Petersburg State Polytechnical University, St. Petersburg, 195251, Russian Federation},
abstract={Five mutant forms of glucoamylase (GA) from the filamentous fungus Aspergillus awamori with artificial disulfide bonds (4D-G137A\A14C, 6D-A14C\Y419C\G137A, 10D-V13C\G396C, 11D-V13C\G396C\A14C\Y419C\G137A, and 20D-G137A\A246C\A14C) were constructed using molecular modeling simulations and experimentally tested for thermostability. The introduction of two additional disulfide bonds between its first and thirteenth α-helices and that of the loop located close to a catalytic residue-E400-made it possible to assess the effects of disulfide bridges on protein thermostability. The mutant proteins with combined amino acid substitutions G137A\A14C, V13C\G396C\A14C\Y419C\G137A, and G137A\A246C\A14C showed higher thermal stability as compared to the wild-type protein. At the same time, new disulfide bridges in the mutant A14C\Y419C\G137A and V13C\G396C proteins led to the destabilization of their structure and the loss of thermal stability. © 2014 Pleiades Publishing, Inc.},
correspondence_address1={Surzhik, M. A.; Konstantinov Institute of Nuclear Physics, National Research Centre Kurchatov Institute, Gatchina, Leningrad oblast, 188300, Russian Federation; email: pmg@omrb.pnpi.spb.ru},
issn={00036838},
language={English},
abbrev_source_title={Appl. Biochem. Microbiol.},
document_type={Article},
source={Scopus},
}
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