Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities

Autores
Joyet, Philippe; Mokhtari, Abdelhamid; Riboulet-Bisson, Eliette; Blancato, Victor Sebastian; Espariz, Martin; Magni, Christian; Hartke, Axel; Deutscher, Josef; Sauvageot, Nicolas
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by α-1,4- but also some α-1,6-linked glucosyl residues. The α-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In Enterococcus faecalis, maltotriose is mainly transported and phosphorylated by a phosphoenolpyruvate:carbohydrate phosphotransferase system. The formed maltotriose-6α-phosphate is intracellularly dephosphorylated by a specific phosphatase, MapP. In contrast, maltotetraose and longer maltooligosaccharides up to maltoheptaose are taken up without phosphorylation via the ATP binding cassette transporter MdxEFG-MsmX. We show that the maltose-producing maltodextrin hydrolase MmdH (GenBank accession no. EFT41964) in strain JH2-2 catalyzes the first catabolic step of α-1,4-linked maltooligosaccharides. The purified enzyme converts even-numbered α-1,4-linked maltooligosaccharides (maltotetraose, etc.) into maltose and odd-numbered (maltotriose, etc.) into maltose and glucose. Inactivation of mmdH therefore prevents the growth of E. faecalis on maltooligosaccharides ranging from maltotriose to maltoheptaose. Surprisingly, MmdH also functions as a maltogenic α-1,6-glucosidase, because it converts the maltotriose isomer isopanose into maltose and glucose. In addition, E. faecalis contains a glucose-producing α-1,6- specific maltodextrin hydrolase (GenBank accession no. EFT41963, renamed GmdH). This enzyme converts panose, another maltotriose isomer, into glucose and maltose. A gmdH mutant had therefore lost the capacity to grow on panose. The genes mmdH and gmdH are organized in an operon together with GenBank accession no. EFT41962 (renamed mmgT). Purified MmgT transfers glucosyl residues from one α-1,4-linked maltooligosaccharide molecule to another. For example, it catalyzes the disproportionation of maltotriose by transferring a glucosyl residue to another maltotriose molecule, thereby forming maltotetraose and maltose together with a small amount of maltopentaose.
Fil: Joyet, Philippe. Université Paris-Saclay; Francia
Fil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. 8 May 1945 University; Argelia
Fil: Riboulet-Bisson, Eliette. Normandie University; Francia
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Espariz, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Hartke, Axel. Normandie University; Francia
Fil: Deutscher, Josef. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Sauvageot, Nicolas. Normandie University; Francia
Materia
ENTEROCOCCUS FAECALIS
GLUCOSYL TRANSFERASE
MALTODEXTRIN CATABOLISM
Α-1,4-GLUCOSIDASE
Α-1,6-GLUCOSIDASE
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:11336/65903
Acceder
id CONICETDig_5341fcee139662f0540e694176953c3e
oai_identifier_str oai:ri.conicet.gov.ar:11336/65903
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activitiesJoyet, PhilippeMokhtari, AbdelhamidRiboulet-Bisson, ElietteBlancato, Victor SebastianEspariz, MartinMagni, ChristianHartke, AxelDeutscher, JosefSauvageot, NicolasENTEROCOCCUS FAECALISGLUCOSYL TRANSFERASEMALTODEXTRIN CATABOLISMΑ-1,4-GLUCOSIDASEΑ-1,6-GLUCOSIDASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by α-1,4- but also some α-1,6-linked glucosyl residues. The α-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In Enterococcus faecalis, maltotriose is mainly transported and phosphorylated by a phosphoenolpyruvate:carbohydrate phosphotransferase system. The formed maltotriose-6α-phosphate is intracellularly dephosphorylated by a specific phosphatase, MapP. In contrast, maltotetraose and longer maltooligosaccharides up to maltoheptaose are taken up without phosphorylation via the ATP binding cassette transporter MdxEFG-MsmX. We show that the maltose-producing maltodextrin hydrolase MmdH (GenBank accession no. EFT41964) in strain JH2-2 catalyzes the first catabolic step of α-1,4-linked maltooligosaccharides. The purified enzyme converts even-numbered α-1,4-linked maltooligosaccharides (maltotetraose, etc.) into maltose and odd-numbered (maltotriose, etc.) into maltose and glucose. Inactivation of mmdH therefore prevents the growth of E. faecalis on maltooligosaccharides ranging from maltotriose to maltoheptaose. Surprisingly, MmdH also functions as a maltogenic α-1,6-glucosidase, because it converts the maltotriose isomer isopanose into maltose and glucose. In addition, E. faecalis contains a glucose-producing α-1,6- specific maltodextrin hydrolase (GenBank accession no. EFT41963, renamed GmdH). This enzyme converts panose, another maltotriose isomer, into glucose and maltose. A gmdH mutant had therefore lost the capacity to grow on panose. The genes mmdH and gmdH are organized in an operon together with GenBank accession no. EFT41962 (renamed mmgT). Purified MmgT transfers glucosyl residues from one α-1,4-linked maltooligosaccharide molecule to another. For example, it catalyzes the disproportionation of maltotriose by transferring a glucosyl residue to another maltotriose molecule, thereby forming maltotetraose and maltose together with a small amount of maltopentaose.Fil: Joyet, Philippe. Université Paris-Saclay; FranciaFil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. 8 May 1945 University; ArgeliaFil: Riboulet-Bisson, Eliette. Normandie University; FranciaFil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Espariz, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Hartke, Axel. Normandie University; FranciaFil: Deutscher, Josef. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; FranciaFil: Sauvageot, Nicolas. Normandie University; FranciaAmerican Society for Microbiology2017-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/65903Joyet, Philippe; Mokhtari, Abdelhamid; Riboulet-Bisson, Eliette; Blancato, Victor Sebastian; Espariz, Martin; et al.; Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities; American Society for Microbiology; Applied And Environmental Microbiology; 83; 13; 7-20170099-2240CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.00038-17info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/83/13/e00038-17info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:28:31Zoai:ri.conicet.gov.ar:11336/65903instacron: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:34982025-10-22 11:28:31.581CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
title Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
spellingShingle Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
Joyet, Philippe
ENTEROCOCCUS FAECALIS
GLUCOSYL TRANSFERASE
MALTODEXTRIN CATABOLISM
Α-1,4-GLUCOSIDASE
Α-1,6-GLUCOSIDASE
title_short Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
title_full Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
title_fullStr Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
title_full_unstemmed Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
title_sort Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities
dc.creator.none.fl_str_mv Joyet, Philippe
Mokhtari, Abdelhamid
Riboulet-Bisson, Eliette
Blancato, Victor Sebastian
Espariz, Martin
Magni, Christian
Hartke, Axel
Deutscher, Josef
Sauvageot, Nicolas
author Joyet, Philippe
author_facet Joyet, Philippe
Mokhtari, Abdelhamid
Riboulet-Bisson, Eliette
Blancato, Victor Sebastian
Espariz, Martin
Magni, Christian
Hartke, Axel
Deutscher, Josef
Sauvageot, Nicolas
author_role author
author2 Mokhtari, Abdelhamid
Riboulet-Bisson, Eliette
Blancato, Victor Sebastian
Espariz, Martin
Magni, Christian
Hartke, Axel
Deutscher, Josef
Sauvageot, Nicolas
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ENTEROCOCCUS FAECALIS
GLUCOSYL TRANSFERASE
MALTODEXTRIN CATABOLISM
Α-1,4-GLUCOSIDASE
Α-1,6-GLUCOSIDASE
topic ENTEROCOCCUS FAECALIS
GLUCOSYL TRANSFERASE
MALTODEXTRIN CATABOLISM
Α-1,4-GLUCOSIDASE
Α-1,6-GLUCOSIDASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by α-1,4- but also some α-1,6-linked glucosyl residues. The α-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In Enterococcus faecalis, maltotriose is mainly transported and phosphorylated by a phosphoenolpyruvate:carbohydrate phosphotransferase system. The formed maltotriose-6α-phosphate is intracellularly dephosphorylated by a specific phosphatase, MapP. In contrast, maltotetraose and longer maltooligosaccharides up to maltoheptaose are taken up without phosphorylation via the ATP binding cassette transporter MdxEFG-MsmX. We show that the maltose-producing maltodextrin hydrolase MmdH (GenBank accession no. EFT41964) in strain JH2-2 catalyzes the first catabolic step of α-1,4-linked maltooligosaccharides. The purified enzyme converts even-numbered α-1,4-linked maltooligosaccharides (maltotetraose, etc.) into maltose and odd-numbered (maltotriose, etc.) into maltose and glucose. Inactivation of mmdH therefore prevents the growth of E. faecalis on maltooligosaccharides ranging from maltotriose to maltoheptaose. Surprisingly, MmdH also functions as a maltogenic α-1,6-glucosidase, because it converts the maltotriose isomer isopanose into maltose and glucose. In addition, E. faecalis contains a glucose-producing α-1,6- specific maltodextrin hydrolase (GenBank accession no. EFT41963, renamed GmdH). This enzyme converts panose, another maltotriose isomer, into glucose and maltose. A gmdH mutant had therefore lost the capacity to grow on panose. The genes mmdH and gmdH are organized in an operon together with GenBank accession no. EFT41962 (renamed mmgT). Purified MmgT transfers glucosyl residues from one α-1,4-linked maltooligosaccharide molecule to another. For example, it catalyzes the disproportionation of maltotriose by transferring a glucosyl residue to another maltotriose molecule, thereby forming maltotetraose and maltose together with a small amount of maltopentaose.
Fil: Joyet, Philippe. Université Paris-Saclay; Francia
Fil: Mokhtari, Abdelhamid. Université Paris-Saclay; Francia. 8 May 1945 University; Argelia
Fil: Riboulet-Bisson, Eliette. Normandie University; Francia
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Espariz, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Hartke, Axel. Normandie University; Francia
Fil: Deutscher, Josef. Université Paris-Saclay; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Sauvageot, Nicolas. Normandie University; Francia
description Maltose and maltodextrins are formed during the degradation of starch or glycogen. Maltodextrins are composed of a mixture of maltooligosaccharides formed by α-1,4- but also some α-1,6-linked glucosyl residues. The α-1,6-linked glucosyl residues are derived from branching points in the polysaccharides. In Enterococcus faecalis, maltotriose is mainly transported and phosphorylated by a phosphoenolpyruvate:carbohydrate phosphotransferase system. The formed maltotriose-6α-phosphate is intracellularly dephosphorylated by a specific phosphatase, MapP. In contrast, maltotetraose and longer maltooligosaccharides up to maltoheptaose are taken up without phosphorylation via the ATP binding cassette transporter MdxEFG-MsmX. We show that the maltose-producing maltodextrin hydrolase MmdH (GenBank accession no. EFT41964) in strain JH2-2 catalyzes the first catabolic step of α-1,4-linked maltooligosaccharides. The purified enzyme converts even-numbered α-1,4-linked maltooligosaccharides (maltotetraose, etc.) into maltose and odd-numbered (maltotriose, etc.) into maltose and glucose. Inactivation of mmdH therefore prevents the growth of E. faecalis on maltooligosaccharides ranging from maltotriose to maltoheptaose. Surprisingly, MmdH also functions as a maltogenic α-1,6-glucosidase, because it converts the maltotriose isomer isopanose into maltose and glucose. In addition, E. faecalis contains a glucose-producing α-1,6- specific maltodextrin hydrolase (GenBank accession no. EFT41963, renamed GmdH). This enzyme converts panose, another maltotriose isomer, into glucose and maltose. A gmdH mutant had therefore lost the capacity to grow on panose. The genes mmdH and gmdH are organized in an operon together with GenBank accession no. EFT41962 (renamed mmgT). Purified MmgT transfers glucosyl residues from one α-1,4-linked maltooligosaccharide molecule to another. For example, it catalyzes the disproportionation of maltotriose by transferring a glucosyl residue to another maltotriose molecule, thereby forming maltotetraose and maltose together with a small amount of maltopentaose.
publishDate 2017
dc.date.none.fl_str_mv 2017-07
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/11336/65903
Joyet, Philippe; Mokhtari, Abdelhamid; Riboulet-Bisson, Eliette; Blancato, Victor Sebastian; Espariz, Martin; et al.; Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities; American Society for Microbiology; Applied And Environmental Microbiology; 83; 13; 7-2017
0099-2240
CONICET Digital
CONICET
url http://hdl.handle.net/11336/65903
identifier_str_mv Joyet, Philippe; Mokhtari, Abdelhamid; Riboulet-Bisson, Eliette; Blancato, Victor Sebastian; Espariz, Martin; et al.; Enzymes required for maltodextrin catabolism in Enterococcus faecalis exhibit novel activities; American Society for Microbiology; Applied And Environmental Microbiology; 83; 13; 7-2017
0099-2240
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.00038-17
info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/83/13/e00038-17
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
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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