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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/65903
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/65903 |
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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 Técnicas2025-09-29T09:59:10Zoai: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:34982025-09-29 09:59:11.068CONICET 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) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1844613757417816064 |
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13.070432 |