An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position
International audience The presence of aminoacylase activities was investigated in a crude extract of Streptomyces ambofaciens ATCC23877.First activities catalyzing the hydrolysis of N-alpha or epsilon-acetyl-L-lysine were identified. Furthermore, the acylation of lysine and different peptides was s...
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Online Access: | https://hal.archives-ouvertes.fr/hal-01959650 https://doi.org/10.1002/elsc.201700173 |
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ftccsdartic:oai:HAL:hal-01959650v1 2023-05-15T14:02:13+02:00 An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position Dettori, Léna Ferrari, Florent Framboisier, Xavier Paris, Cédric Guiavarc’h, Yann Hotel, Laurence Aymes, Arnaud Leblond, Pierre Humeau, Catherine Kapel, Romain Chevalot, Isabelle Aigle, Bertrand Delaunay, Stéphane Laboratoire Réactions et Génie des Procédés (LRGP) Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL) Plateau d’Analyse Structurale et Métabolomique (PASM) Université de Lorraine (UL) Dynamique des Génomes et Adaptation Microbienne (DynAMic) Université de Lorraine (UL)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) "impact biomolecules" project of the "Lorraine Universite d'Excellence" (PIA-ANR) French National Research Agency (ANR) through the "ISEAPIM3" project ANR-15-CE07-0023-01 "Structure Federative de Recherche Ecosystemes Forestiers, Agroressources, Bioprocedes et Alimentation" of the University of Lorraine "Region Lorraine" European Union through the "Programme Operationnel FEDER FSE Lorraine et Massif des Vosges 2014-2020" IMPACT BIOMOLECULES ANR-15-IDEX-0004,LUE,Isite LUE(2015) ANR-15-CE07-0023,ISEAPIM3,Procédé Intensifié et Durable d'Acylation Enzymatique sur Materiaux Macroporeux/Mesoporeux Innovants(2015) 2018 https://hal.archives-ouvertes.fr/hal-01959650 https://doi.org/10.1002/elsc.201700173 en eng HAL CCSD Wiley-VCH Verlag info:eu-repo/semantics/altIdentifier/doi/10.1002/elsc.201700173 hal-01959650 https://hal.archives-ouvertes.fr/hal-01959650 doi:10.1002/elsc.201700173 PRODINRA: 456089 WOS: 000440549100007 ISSN: 1618-0240 EISSN: 1618-2863 Engineering in Life Sciences https://hal.archives-ouvertes.fr/hal-01959650 Engineering in Life Sciences, Wiley-VCH Verlag, 2018, 18 (8), pp.589-599. ⟨10.1002/elsc.201700173⟩ https://onlinelibrary.wiley.com/journal/16182863 L-AMINO ACIDS ACYLASE LINEAR CHROMOSOME ENZYMATIC-SYNTHESIS MOBARAENSIS SURFACTANTS ESCHERICHIA-COLI PURIFICATION BIOSYNTHESIS GENES aminoacylation peptide Candida antarctica B streptomyces ambofaciens [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2018 ftccsdartic https://doi.org/10.1002/elsc.201700173 2021-11-07T02:26:22Z International audience The presence of aminoacylase activities was investigated in a crude extract of Streptomyces ambofaciens ATCC23877.First activities catalyzing the hydrolysis of N-alpha or epsilon-acetyl-L-lysine were identified. Furthermore, the acylation of lysine and different peptides was studied and compared with results obtained with lipase B of Candida antarctica (CALB). Different regioselectivities were demonstrated for the two classes of enzymes.CALB was able to catalyze acylation only on the epsilon-position whereas the crude extract from S. ambofaciens possessed the rare ability to catalyze the N-acylation on the alpha-position of the lysine or of the amino-acid in N-terminal position of peptides. Two genes, SAM23877_1485 and SAM23877_1734, were identified in the genome of Streptomyces ambofaciens ATCC23877 whose products show similarities with the previously identified aminoacylases from Streptomyces mobaraensis.The proteins encoded by these two genes were responsible for the major aminoacylase hydrolytic activities. Furthermore, we show that the hydrolysis of N-alpha-acetyl-L-lysine could be attributed to the product of SAM23877_1734 gene. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Engineering in Life Sciences 18 8 589 599 |
institution |
Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
L-AMINO ACIDS ACYLASE LINEAR CHROMOSOME ENZYMATIC-SYNTHESIS MOBARAENSIS SURFACTANTS ESCHERICHIA-COLI PURIFICATION BIOSYNTHESIS GENES aminoacylation peptide Candida antarctica B streptomyces ambofaciens [SDV]Life Sciences [q-bio] |
spellingShingle |
L-AMINO ACIDS ACYLASE LINEAR CHROMOSOME ENZYMATIC-SYNTHESIS MOBARAENSIS SURFACTANTS ESCHERICHIA-COLI PURIFICATION BIOSYNTHESIS GENES aminoacylation peptide Candida antarctica B streptomyces ambofaciens [SDV]Life Sciences [q-bio] Dettori, Léna Ferrari, Florent Framboisier, Xavier Paris, Cédric Guiavarc’h, Yann Hotel, Laurence Aymes, Arnaud Leblond, Pierre Humeau, Catherine Kapel, Romain Chevalot, Isabelle Aigle, Bertrand Delaunay, Stéphane An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
topic_facet |
L-AMINO ACIDS ACYLASE LINEAR CHROMOSOME ENZYMATIC-SYNTHESIS MOBARAENSIS SURFACTANTS ESCHERICHIA-COLI PURIFICATION BIOSYNTHESIS GENES aminoacylation peptide Candida antarctica B streptomyces ambofaciens [SDV]Life Sciences [q-bio] |
description |
International audience The presence of aminoacylase activities was investigated in a crude extract of Streptomyces ambofaciens ATCC23877.First activities catalyzing the hydrolysis of N-alpha or epsilon-acetyl-L-lysine were identified. Furthermore, the acylation of lysine and different peptides was studied and compared with results obtained with lipase B of Candida antarctica (CALB). Different regioselectivities were demonstrated for the two classes of enzymes.CALB was able to catalyze acylation only on the epsilon-position whereas the crude extract from S. ambofaciens possessed the rare ability to catalyze the N-acylation on the alpha-position of the lysine or of the amino-acid in N-terminal position of peptides. Two genes, SAM23877_1485 and SAM23877_1734, were identified in the genome of Streptomyces ambofaciens ATCC23877 whose products show similarities with the previously identified aminoacylases from Streptomyces mobaraensis.The proteins encoded by these two genes were responsible for the major aminoacylase hydrolytic activities. Furthermore, we show that the hydrolysis of N-alpha-acetyl-L-lysine could be attributed to the product of SAM23877_1734 gene. |
author2 |
Laboratoire Réactions et Génie des Procédés (LRGP) Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL) Plateau d’Analyse Structurale et Métabolomique (PASM) Université de Lorraine (UL) Dynamique des Génomes et Adaptation Microbienne (DynAMic) Université de Lorraine (UL)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) "impact biomolecules" project of the "Lorraine Universite d'Excellence" (PIA-ANR) French National Research Agency (ANR) through the "ISEAPIM3" project ANR-15-CE07-0023-01 "Structure Federative de Recherche Ecosystemes Forestiers, Agroressources, Bioprocedes et Alimentation" of the University of Lorraine "Region Lorraine" European Union through the "Programme Operationnel FEDER FSE Lorraine et Massif des Vosges 2014-2020" IMPACT BIOMOLECULES ANR-15-IDEX-0004,LUE,Isite LUE(2015) ANR-15-CE07-0023,ISEAPIM3,Procédé Intensifié et Durable d'Acylation Enzymatique sur Materiaux Macroporeux/Mesoporeux Innovants(2015) |
format |
Article in Journal/Newspaper |
author |
Dettori, Léna Ferrari, Florent Framboisier, Xavier Paris, Cédric Guiavarc’h, Yann Hotel, Laurence Aymes, Arnaud Leblond, Pierre Humeau, Catherine Kapel, Romain Chevalot, Isabelle Aigle, Bertrand Delaunay, Stéphane |
author_facet |
Dettori, Léna Ferrari, Florent Framboisier, Xavier Paris, Cédric Guiavarc’h, Yann Hotel, Laurence Aymes, Arnaud Leblond, Pierre Humeau, Catherine Kapel, Romain Chevalot, Isabelle Aigle, Bertrand Delaunay, Stéphane |
author_sort |
Dettori, Léna |
title |
An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
title_short |
An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
title_full |
An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
title_fullStr |
An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
title_full_unstemmed |
An aminoacylase activity from Streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on N-terminal position |
title_sort |
aminoacylase activity from streptomyces ambofaciens catalyzes the acylation of lysine on α-position and peptides on n-terminal position |
publisher |
HAL CCSD |
publishDate |
2018 |
url |
https://hal.archives-ouvertes.fr/hal-01959650 https://doi.org/10.1002/elsc.201700173 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1618-0240 EISSN: 1618-2863 Engineering in Life Sciences https://hal.archives-ouvertes.fr/hal-01959650 Engineering in Life Sciences, Wiley-VCH Verlag, 2018, 18 (8), pp.589-599. ⟨10.1002/elsc.201700173⟩ https://onlinelibrary.wiley.com/journal/16182863 |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1002/elsc.201700173 hal-01959650 https://hal.archives-ouvertes.fr/hal-01959650 doi:10.1002/elsc.201700173 PRODINRA: 456089 WOS: 000440549100007 |
op_doi |
https://doi.org/10.1002/elsc.201700173 |
container_title |
Engineering in Life Sciences |
container_volume |
18 |
container_issue |
8 |
container_start_page |
589 |
op_container_end_page |
599 |
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1766272339955154944 |