The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium
Publication type: Journal Article
Publication date: 2015-02-01
SJR: —
CiteScore: —
Impact factor: —
ISSN: 13811177
Catalysis
Biochemistry
Process Chemistry and Technology
Bioengineering
Abstract
The computationally designed βD484N mutant of penicillin acylase from Escherichia coli was shown to be more stable at alkaline conditions, resistant to inactivation by high substrate concentrations and able to catalyze preparative peptide synthesis in aqueous medium more effectively. The ability of the βD484N mutant to operate in alkaline aqueous medium allowed to reach up to 80% yields of d -phenylglycine-derived peptide synthesis from equimolar substrate mixtures while with the wild type penicillin acylase conversion was below 17%.
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Shcherbakova T. A. et al. The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium // Journal of Molecular Catalysis B Enzymatic. 2015. Vol. 112. pp. 66-68.
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Shcherbakova T. A., Panin N. V., Suplatov D., Shapovalova I. V., Švedas V. K. The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium // Journal of Molecular Catalysis B Enzymatic. 2015. Vol. 112. pp. 66-68.
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TY - JOUR
DO - 10.1016/j.molcatb.2014.11.015
UR - https://doi.org/10.1016/j.molcatb.2014.11.015
TI - The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium
T2 - Journal of Molecular Catalysis B Enzymatic
AU - Shcherbakova, Tatyana A.
AU - Panin, Nikolay V
AU - Suplatov, Dmitry
AU - Shapovalova, Irina V
AU - Švedas, Vytas K.
PY - 2015
DA - 2015/02/01
PB - Elsevier
SP - 66-68
VL - 112
SN - 1381-1177
ER -
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@article{2015_Shcherbakova,
author = {Tatyana A. Shcherbakova and Nikolay V Panin and Dmitry Suplatov and Irina V Shapovalova and Vytas K. Švedas},
title = {The βD484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium},
journal = {Journal of Molecular Catalysis B Enzymatic},
year = {2015},
volume = {112},
publisher = {Elsevier},
month = {feb},
url = {https://doi.org/10.1016/j.molcatb.2014.11.015},
pages = {66--68},
doi = {10.1016/j.molcatb.2014.11.015}
}