Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III

Autores
Gomez Casati, Diego Fabian; Martín, Mariana; Busi, María Victoria
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glycosyltransferases (GTs) are a ubiquitous group of enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Nucleotide-sugars, lipid phosphate sugars and phosphate sugars can act as activated donor molecules while acceptor substrates involve carbohydrates, proteins, lipids, DNA and also, numerous small molecules (i. e. antibiotics, flavonols, steroids). GTs enzyme families are very ancient. They are founded in all the three domains of life and display three different folds (named GT-A, GTB and GT-C) which are a variant of a common α/β scaffold. In addition, several GTs contain an associated non-catalytic carbohydrate binding module (CBM) that could be critical for enzyme activity.
This work reviews the current knowledge on the GTs structures and functions and highlights those enzymes that contain CBMs, particularly starch binding domains (SBDs). In addition, we also focus on A. thaliana starch synthase III enzyme, from the GT-5 family. This protein has a GT-B fold, and contains in its N-terminal region three in tandem SBDs, which are essential for the regulation of enzyme activity.
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Martín, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Materia
Carbohydrate Binding Modules
Glycosyltransferases
Starch Binding Domains
Starch Synthase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/3436
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase IIIGomez Casati, Diego FabianMartín, MarianaBusi, María VictoriaCarbohydrate Binding ModulesGlycosyltransferasesStarch Binding DomainsStarch Synthasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glycosyltransferases (GTs) are a ubiquitous group of enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Nucleotide-sugars, lipid phosphate sugars and phosphate sugars can act as activated donor molecules while acceptor substrates involve carbohydrates, proteins, lipids, DNA and also, numerous small molecules (i. e. antibiotics, flavonols, steroids). GTs enzyme families are very ancient. They are founded in all the three domains of life and display three different folds (named GT-A, GTB and GT-C) which are a variant of a common α/β scaffold. In addition, several GTs contain an associated non-catalytic carbohydrate binding module (CBM) that could be critical for enzyme activity.<br />This work reviews the current knowledge on the GTs structures and functions and highlights those enzymes that contain CBMs, particularly starch binding domains (SBDs). In addition, we also focus on A. thaliana starch synthase III enzyme, from the GT-5 family. This protein has a GT-B fold, and contains in its N-terminal region three in tandem SBDs, which are essential for the regulation of enzyme activity.Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaFil: Martín, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; ArgentinaBentham Science Publishers2013-05info: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/11336/3436Gomez Casati, Diego Fabian; Martín, Mariana; Busi, María Victoria; Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III; Bentham Science Publishers; Protein And Peptide Letters; 20; 5-2013; 856-8630929-8665enginfo:eu-repo/semantics/altIdentifier/url/http://www.benthamscience.com/ppl/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:54Zoai:ri.conicet.gov.ar:11336/3436instacron: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:34982025-09-03 09:44:54.389CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
title Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
spellingShingle Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
Gomez Casati, Diego Fabian
Carbohydrate Binding Modules
Glycosyltransferases
Starch Binding Domains
Starch Synthase
title_short Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
title_full Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
title_fullStr Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
title_full_unstemmed Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
title_sort Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III
dc.creator.none.fl_str_mv Gomez Casati, Diego Fabian
Martín, Mariana
Busi, María Victoria
author Gomez Casati, Diego Fabian
author_facet Gomez Casati, Diego Fabian
Martín, Mariana
Busi, María Victoria
author_role author
author2 Martín, Mariana
Busi, María Victoria
author2_role author
author
dc.subject.none.fl_str_mv Carbohydrate Binding Modules
Glycosyltransferases
Starch Binding Domains
Starch Synthase
topic Carbohydrate Binding Modules
Glycosyltransferases
Starch Binding Domains
Starch Synthase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Glycosyltransferases (GTs) are a ubiquitous group of enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Nucleotide-sugars, lipid phosphate sugars and phosphate sugars can act as activated donor molecules while acceptor substrates involve carbohydrates, proteins, lipids, DNA and also, numerous small molecules (i. e. antibiotics, flavonols, steroids). GTs enzyme families are very ancient. They are founded in all the three domains of life and display three different folds (named GT-A, GTB and GT-C) which are a variant of a common α/β scaffold. In addition, several GTs contain an associated non-catalytic carbohydrate binding module (CBM) that could be critical for enzyme activity.<br />This work reviews the current knowledge on the GTs structures and functions and highlights those enzymes that contain CBMs, particularly starch binding domains (SBDs). In addition, we also focus on A. thaliana starch synthase III enzyme, from the GT-5 family. This protein has a GT-B fold, and contains in its N-terminal region three in tandem SBDs, which are essential for the regulation of enzyme activity.
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Martín, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina
description Glycosyltransferases (GTs) are a ubiquitous group of enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Nucleotide-sugars, lipid phosphate sugars and phosphate sugars can act as activated donor molecules while acceptor substrates involve carbohydrates, proteins, lipids, DNA and also, numerous small molecules (i. e. antibiotics, flavonols, steroids). GTs enzyme families are very ancient. They are founded in all the three domains of life and display three different folds (named GT-A, GTB and GT-C) which are a variant of a common α/β scaffold. In addition, several GTs contain an associated non-catalytic carbohydrate binding module (CBM) that could be critical for enzyme activity.<br />This work reviews the current knowledge on the GTs structures and functions and highlights those enzymes that contain CBMs, particularly starch binding domains (SBDs). In addition, we also focus on A. thaliana starch synthase III enzyme, from the GT-5 family. This protein has a GT-B fold, and contains in its N-terminal region three in tandem SBDs, which are essential for the regulation of enzyme activity.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/3436
Gomez Casati, Diego Fabian; Martín, Mariana; Busi, María Victoria; Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III; Bentham Science Publishers; Protein And Peptide Letters; 20; 5-2013; 856-863
0929-8665
url http://hdl.handle.net/11336/3436
identifier_str_mv Gomez Casati, Diego Fabian; Martín, Mariana; Busi, María Victoria; Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III; Bentham Science Publishers; Protein And Peptide Letters; 20; 5-2013; 856-863
0929-8665
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.benthamscience.com/ppl/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/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 Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
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 13.13397

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