The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase

Autores
Landete, José M.; Arena, Mario Eduardo; Pardo, Isabel; Manca de Nadra, María C.; Ferrer, Sergi
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Putrescine, one of the main biogenic amines associated to microbial food spoilage, can be formed by bacteria from arginine via ornithine decarboxylase (ODC), or from agmatine via agmatine deiminase (AgDI). This study aims to correlate putrescine production from agmatine to the pathway involving N-carbamoylputrescine formation via AdDI (the aguA product) and N-carbamoylputrescine amidohydrolase (the aguB product), or putrescine carbamoyltransferase (the ptcA product) in bacteria. PCR methods were developed to detect the two genes involved in putrescine production from agmatine. Putrescine production from agmatine could be linked to the aguA and ptcA genes in Lactobacillus hilgardii X1B, Enterococcus faecalis ATCC 11700, and Bacillus cereus ATCC 14579. By contrast Lactobacillus sakei 23K was unable to produce putrescine, and although a fragment of DNA corresponding to the gene aguA was amplified, no amplification was observed for the ptcA gene. Pseudomonas aeruginosa PAO1 produces putrescine and is reported to harbour aguA and aguB genes, responsible for agmatine deiminase and N-carbamoylputrescine amidohydrolase activities. The enzyme from P. aeruginosa PAO1 that converts N-carbamoylputrescine to putrescine (the aguB product) is different from other microorganisms studied (the ptcA product). Therefore, the aguB gene from P. aeruginosa PAO1 could not be amplified with ptcA-specific primers. The aguB and ptcA genes have frequently been erroneously annotated in the past, as in fact these two enzymes are neither homologous nor analogous. Furthermore, the aguA, aguB and ptcA sequences available from GenBank were subjected to phylogenetic analysis, revealing that gram-positive bacteria harboured ptcA, whereas gram-negative bacteria harbour aguB. This paper also discusses the role of the agmatine deiminase system (AgDS) in acid stress resistance.
Fil: Landete, José M.. Universidad de Valencia; España
Fil: Arena, Mario Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Pardo, Isabel. Universidad de Valencia; España
Fil: Manca de Nadra, María C.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Ferrer, Sergi. Universidad de Valencia; España
Materia
AGMATINE
AGMATINE DEIMINASE
N-CARBAMOYLPUTRESCINE AMIDOHYDROLASE
PUTRESCINE
PUTRESCINE CARBAMOYLTRANSFERASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/52504
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/52504
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminaseLandete, José M.Arena, Mario EduardoPardo, IsabelManca de Nadra, María C.Ferrer, SergiAGMATINEAGMATINE DEIMINASEN-CARBAMOYLPUTRESCINE AMIDOHYDROLASEPUTRESCINEPUTRESCINE CARBAMOYLTRANSFERASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Putrescine, one of the main biogenic amines associated to microbial food spoilage, can be formed by bacteria from arginine via ornithine decarboxylase (ODC), or from agmatine via agmatine deiminase (AgDI). This study aims to correlate putrescine production from agmatine to the pathway involving N-carbamoylputrescine formation via AdDI (the aguA product) and N-carbamoylputrescine amidohydrolase (the aguB product), or putrescine carbamoyltransferase (the ptcA product) in bacteria. PCR methods were developed to detect the two genes involved in putrescine production from agmatine. Putrescine production from agmatine could be linked to the aguA and ptcA genes in Lactobacillus hilgardii X1B, Enterococcus faecalis ATCC 11700, and Bacillus cereus ATCC 14579. By contrast Lactobacillus sakei 23K was unable to produce putrescine, and although a fragment of DNA corresponding to the gene aguA was amplified, no amplification was observed for the ptcA gene. Pseudomonas aeruginosa PAO1 produces putrescine and is reported to harbour aguA and aguB genes, responsible for agmatine deiminase and N-carbamoylputrescine amidohydrolase activities. The enzyme from P. aeruginosa PAO1 that converts N-carbamoylputrescine to putrescine (the aguB product) is different from other microorganisms studied (the ptcA product). Therefore, the aguB gene from P. aeruginosa PAO1 could not be amplified with ptcA-specific primers. The aguB and ptcA genes have frequently been erroneously annotated in the past, as in fact these two enzymes are neither homologous nor analogous. Furthermore, the aguA, aguB and ptcA sequences available from GenBank were subjected to phylogenetic analysis, revealing that gram-positive bacteria harboured ptcA, whereas gram-negative bacteria harbour aguB. This paper also discusses the role of the agmatine deiminase system (AgDS) in acid stress resistance.Fil: Landete, José M.. Universidad de Valencia; EspañaFil: Arena, Mario Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Pardo, Isabel. Universidad de Valencia; EspañaFil: Manca de Nadra, María C.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Ferrer, Sergi. Universidad de Valencia; EspañaSociedad Española de Microbiología2010-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/52504Landete, José M.; Arena, Mario Eduardo; Pardo, Isabel; Manca de Nadra, María C.; Ferrer, Sergi; The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase; Sociedad Española de Microbiología; International Microbiology; 13; 4; 12-2010; 169-1771139-67091618-1905CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.2436/20.1501.01.123info:eu-repo/semantics/altIdentifier/url/http://revistes.iec.cat/index.php/IM/article/view/53871info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:30:24Zoai:ri.conicet.gov.ar:11336/52504instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:30:25.22CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
title The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
spellingShingle The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
Landete, José M.
AGMATINE
AGMATINE DEIMINASE
N-CARBAMOYLPUTRESCINE AMIDOHYDROLASE
PUTRESCINE
PUTRESCINE CARBAMOYLTRANSFERASE
title_short The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
title_full The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
title_fullStr The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
title_full_unstemmed The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
title_sort The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
dc.creator.none.fl_str_mv Landete, José M.
Arena, Mario Eduardo
Pardo, Isabel
Manca de Nadra, María C.
Ferrer, Sergi
author Landete, José M.
author_facet Landete, José M.
Arena, Mario Eduardo
Pardo, Isabel
Manca de Nadra, María C.
Ferrer, Sergi
author_role author
author2 Arena, Mario Eduardo
Pardo, Isabel
Manca de Nadra, María C.
Ferrer, Sergi
author2_role author
author
author
author
dc.subject.none.fl_str_mv AGMATINE
AGMATINE DEIMINASE
N-CARBAMOYLPUTRESCINE AMIDOHYDROLASE
PUTRESCINE
PUTRESCINE CARBAMOYLTRANSFERASE
topic AGMATINE
AGMATINE DEIMINASE
N-CARBAMOYLPUTRESCINE AMIDOHYDROLASE
PUTRESCINE
PUTRESCINE CARBAMOYLTRANSFERASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Putrescine, one of the main biogenic amines associated to microbial food spoilage, can be formed by bacteria from arginine via ornithine decarboxylase (ODC), or from agmatine via agmatine deiminase (AgDI). This study aims to correlate putrescine production from agmatine to the pathway involving N-carbamoylputrescine formation via AdDI (the aguA product) and N-carbamoylputrescine amidohydrolase (the aguB product), or putrescine carbamoyltransferase (the ptcA product) in bacteria. PCR methods were developed to detect the two genes involved in putrescine production from agmatine. Putrescine production from agmatine could be linked to the aguA and ptcA genes in Lactobacillus hilgardii X1B, Enterococcus faecalis ATCC 11700, and Bacillus cereus ATCC 14579. By contrast Lactobacillus sakei 23K was unable to produce putrescine, and although a fragment of DNA corresponding to the gene aguA was amplified, no amplification was observed for the ptcA gene. Pseudomonas aeruginosa PAO1 produces putrescine and is reported to harbour aguA and aguB genes, responsible for agmatine deiminase and N-carbamoylputrescine amidohydrolase activities. The enzyme from P. aeruginosa PAO1 that converts N-carbamoylputrescine to putrescine (the aguB product) is different from other microorganisms studied (the ptcA product). Therefore, the aguB gene from P. aeruginosa PAO1 could not be amplified with ptcA-specific primers. The aguB and ptcA genes have frequently been erroneously annotated in the past, as in fact these two enzymes are neither homologous nor analogous. Furthermore, the aguA, aguB and ptcA sequences available from GenBank were subjected to phylogenetic analysis, revealing that gram-positive bacteria harboured ptcA, whereas gram-negative bacteria harbour aguB. This paper also discusses the role of the agmatine deiminase system (AgDS) in acid stress resistance.
Fil: Landete, José M.. Universidad de Valencia; España
Fil: Arena, Mario Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Pardo, Isabel. Universidad de Valencia; España
Fil: Manca de Nadra, María C.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Ferrer, Sergi. Universidad de Valencia; España
description Putrescine, one of the main biogenic amines associated to microbial food spoilage, can be formed by bacteria from arginine via ornithine decarboxylase (ODC), or from agmatine via agmatine deiminase (AgDI). This study aims to correlate putrescine production from agmatine to the pathway involving N-carbamoylputrescine formation via AdDI (the aguA product) and N-carbamoylputrescine amidohydrolase (the aguB product), or putrescine carbamoyltransferase (the ptcA product) in bacteria. PCR methods were developed to detect the two genes involved in putrescine production from agmatine. Putrescine production from agmatine could be linked to the aguA and ptcA genes in Lactobacillus hilgardii X1B, Enterococcus faecalis ATCC 11700, and Bacillus cereus ATCC 14579. By contrast Lactobacillus sakei 23K was unable to produce putrescine, and although a fragment of DNA corresponding to the gene aguA was amplified, no amplification was observed for the ptcA gene. Pseudomonas aeruginosa PAO1 produces putrescine and is reported to harbour aguA and aguB genes, responsible for agmatine deiminase and N-carbamoylputrescine amidohydrolase activities. The enzyme from P. aeruginosa PAO1 that converts N-carbamoylputrescine to putrescine (the aguB product) is different from other microorganisms studied (the ptcA product). Therefore, the aguB gene from P. aeruginosa PAO1 could not be amplified with ptcA-specific primers. The aguB and ptcA genes have frequently been erroneously annotated in the past, as in fact these two enzymes are neither homologous nor analogous. Furthermore, the aguA, aguB and ptcA sequences available from GenBank were subjected to phylogenetic analysis, revealing that gram-positive bacteria harboured ptcA, whereas gram-negative bacteria harbour aguB. This paper also discusses the role of the agmatine deiminase system (AgDS) in acid stress resistance.
publishDate 2010
dc.date.none.fl_str_mv 2010-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/52504
Landete, José M.; Arena, Mario Eduardo; Pardo, Isabel; Manca de Nadra, María C.; Ferrer, Sergi; The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase; Sociedad Española de Microbiología; International Microbiology; 13; 4; 12-2010; 169-177
1139-6709
1618-1905
CONICET Digital
CONICET
url http://hdl.handle.net/11336/52504
identifier_str_mv Landete, José M.; Arena, Mario Eduardo; Pardo, Isabel; Manca de Nadra, María C.; Ferrer, Sergi; The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase; Sociedad Española de Microbiología; International Microbiology; 13; 4; 12-2010; 169-177
1139-6709
1618-1905
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2436/20.1501.01.123
info:eu-repo/semantics/altIdentifier/url/http://revistes.iec.cat/index.php/IM/article/view/53871
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Sociedad Española de Microbiología
publisher.none.fl_str_mv Sociedad Española de Microbiología
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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