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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Bibliographic Details
Published in:Engineering in Life Sciences
Main Authors: 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
Other Authors: 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
Language:English
Published: HAL CCSD 2018
Subjects:
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]
Antarc*
Antarctica
Online Access:https://hal.archives-ouvertes.fr/hal-01959650
https://doi.org/10.1002/elsc.201700173
Description
Summary: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.

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