First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58

Enterococcus faecium RM58 produces b-phenylethylamine and tyramine. A gene from Ent. faecium RM58 coding for a 625 amino-acid residues protein that shows 85% identity to Enterococcus faecalis tyrosine decarboxylase has been expressed in Escherichia coli, resulting in L-phenylalanine and L-tyrosine d...

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Detalles Bibliográficos
Autores: Marcobal, Ángela, De Las Rivas, Blanca, Muñoz, Rosario
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2006
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/45308
Acceso en línea:http://hdl.handle.net/10261/45308
Access Level:acceso abierto
Palabra clave:phenylethylamine
tyramine
decarboxylase
Lactic acid bacteria
Biogenic amines
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spelling First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58Marcobal, ÁngelaDe Las Rivas, BlancaMuñoz, RosariophenylethylaminetyraminedecarboxylaseLactic acid bacteriaBiogenic aminesEnterococcus faecium RM58 produces b-phenylethylamine and tyramine. A gene from Ent. faecium RM58 coding for a 625 amino-acid residues protein that shows 85% identity to Enterococcus faecalis tyrosine decarboxylase has been expressed in Escherichia coli, resulting in L-phenylalanine and L-tyrosine decarboxylase activities. Both activities were lost when a truncated protein lacking 84 amino acids at its C-terminus was expressed in E. coli. This study constitutes the first genetic characterization of a bacterial protein having L-phenylalanine decarboxylase activity and solves a long-standing question regarding the specificity of tyrosine decarboxylases in enterococciThis work was supported by Grant 07G/0035/2003 from the Comunidad de Madrid and RM03-002 from INIA. A. Marcobal was a recipient of a predoctoral fellowship and B. de las Rivas of a postdoctoral fellowship both from the Comunidad de Madrid.Peer reviewedJohn Wiley & SonsComunidad de MadridCSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201220122006info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/45308reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/j.1574-6968.2006.00206.xSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/453082026-05-22T06:33:51Z
dc.title.none.fl_str_mv First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
title First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
spellingShingle First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
Marcobal, Ángela
phenylethylamine
tyramine
decarboxylase
Lactic acid bacteria
Biogenic amines
title_short First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
title_full First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
title_fullStr First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
title_full_unstemmed First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
title_sort First genetic characterization of a bacterial beta-phenylethylamine biosynthetic enzyme in Enterococcus faecium RM58
dc.creator.none.fl_str_mv Marcobal, Ángela
De Las Rivas, Blanca
Muñoz, Rosario
author Marcobal, Ángela
author_facet Marcobal, Ángela
De Las Rivas, Blanca
Muñoz, Rosario
author_role author
author2 De Las Rivas, Blanca
Muñoz, Rosario
author2_role author
author
dc.contributor.none.fl_str_mv Comunidad de Madrid
CSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv phenylethylamine
tyramine
decarboxylase
Lactic acid bacteria
Biogenic amines
topic phenylethylamine
tyramine
decarboxylase
Lactic acid bacteria
Biogenic amines
description Enterococcus faecium RM58 produces b-phenylethylamine and tyramine. A gene from Ent. faecium RM58 coding for a 625 amino-acid residues protein that shows 85% identity to Enterococcus faecalis tyrosine decarboxylase has been expressed in Escherichia coli, resulting in L-phenylalanine and L-tyrosine decarboxylase activities. Both activities were lost when a truncated protein lacking 84 amino acids at its C-terminus was expressed in E. coli. This study constitutes the first genetic characterization of a bacterial protein having L-phenylalanine decarboxylase activity and solves a long-standing question regarding the specificity of tyrosine decarboxylases in enterococci
publishDate 2006
dc.date.none.fl_str_mv 2006
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/45308
url http://hdl.handle.net/10261/45308
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/j.1574-6968.2006.00206.x
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,81155

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