Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans

A unique property was found for oligopeptidase B from Serratia proteamaculans (PSP) as well as its mutants: they can undergo reversible thermal inactivation at 37°C, with activity being restored or even increased with respect to the initial one upon subsequent cooling. The process can be repeated se...

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Autores principales: Ovchinnikova, M. V., Mikhailova, A. G., Karlinsky, D. M., Gorlenko, V. A., Rumsh, L. D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2018
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6087823/
https://www.ncbi.nlm.nih.gov/pubmed/30116617
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author Ovchinnikova, M. V.
Mikhailova, A. G.
Karlinsky, D. M.
Gorlenko, V. A.
Rumsh, L. D.
author_facet Ovchinnikova, M. V.
Mikhailova, A. G.
Karlinsky, D. M.
Gorlenko, V. A.
Rumsh, L. D.
author_sort Ovchinnikova, M. V.
collection PubMed
description A unique property was found for oligopeptidase B from Serratia proteamaculans (PSP) as well as its mutants: they can undergo reversible thermal inactivation at 37°C, with activity being restored or even increased with respect to the initial one upon subsequent cooling. The process can be repeated several times, with the same results achieved (up to 5 cycles). This effect can be explained by a shift in the equilibrium between the inactive open form of the enzyme and the active closed one upon variation of the incubation temperature.
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spelling pubmed-60878232018-08-16 Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans Ovchinnikova, M. V. Mikhailova, A. G. Karlinsky, D. M. Gorlenko, V. A. Rumsh, L. D. Acta Naturae Research Article A unique property was found for oligopeptidase B from Serratia proteamaculans (PSP) as well as its mutants: they can undergo reversible thermal inactivation at 37°C, with activity being restored or even increased with respect to the initial one upon subsequent cooling. The process can be repeated several times, with the same results achieved (up to 5 cycles). This effect can be explained by a shift in the equilibrium between the inactive open form of the enzyme and the active closed one upon variation of the incubation temperature. A.I. Gordeyev 2018 /pmc/articles/PMC6087823/ /pubmed/30116617 Text en Copyright ® 2018 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ovchinnikova, M. V.
Mikhailova, A. G.
Karlinsky, D. M.
Gorlenko, V. A.
Rumsh, L. D.
Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title_full Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title_fullStr Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title_full_unstemmed Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title_short Reversible Cyclic Thermal Inactivation of Oligopeptidase B from Serratia proteamaculans
title_sort reversible cyclic thermal inactivation of oligopeptidase b from serratia proteamaculans
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6087823/
https://www.ncbi.nlm.nih.gov/pubmed/30116617
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