Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation

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Potato (Solanum tuberosum L.) tuber UDP-glucose:protein transglucosylase (UPTG) (EC 2.4.1.112) is involved in the first of a two-step mechanism proposed for protein-bound α-glucan synthesis by catalyzing the covalent attachment of a single glucose residue to an acceptor protein. The resulting glucos...

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Autores principales:	Ardila, F.J., Tandecarz, J.S.
Formato:	Artículo publishedVersion
Publicado:	1992
Materias:	Solanum tuberosum Tuberosum
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00320889_v99_n4_p1342_Ardila http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00320889_v99_n4_p1342_Ardila_oai
Aporte de:	Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

id	I28-R145-paper_00320889_v99_n4_p1342_Ardila_oai
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spelling	I28-R145-paper_00320889_v99_n4_p1342_Ardila_oai2020-10-19 Ardila, F.J. Tandecarz, J.S. 1992 Potato (Solanum tuberosum L.) tuber UDP-glucose:protein transglucosylase (UPTG) (EC 2.4.1.112) is involved in the first of a two-step mechanism proposed for protein-bound α-glucan synthesis by catalyzing the covalent attachment of a single glucose residue to an acceptor protein. The resulting glucosylated 38-kilodalton polypeptide would then serve as a primer for enzymic glucan chain elongation during the second step. In the present report, we describe the fast protein liquid chromatography purification of UPTG from a membrane pellet of potato tuber. An apparently close association of UPTG, phosphorylase, and starch synthase was observed under native conditions during different purification steps. Enrichment of a 38-kilodalton polypeptide was found throughout enzyme purification. It is now shown that the purified UPTG, with an apparent molecular mass of 38 kilodaltons, undergoes self-glucosylation in a UDP-glucose- and Mn2+-dependent reaction. Therefore, it is concluded that UPTG is the enzyme and at the same time the priming protein required for the biogenesis of protein-bound α-glucan in potato tuber. Fil:Ardila, F.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tandecarz, J.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_00320889_v99_n4_p1342_Ardila info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Plant Physiol. 1992;99(4):1342-1347 Solanum tuberosum Tuberosum Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00320889_v99_n4_p1342_Ardila_oai
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-145
collection	Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic	Solanum tuberosum Tuberosum
spellingShingle	Solanum tuberosum Tuberosum Ardila, F.J. Tandecarz, J.S. Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
topic_facet	Solanum tuberosum Tuberosum
description	Potato (Solanum tuberosum L.) tuber UDP-glucose:protein transglucosylase (UPTG) (EC 2.4.1.112) is involved in the first of a two-step mechanism proposed for protein-bound α-glucan synthesis by catalyzing the covalent attachment of a single glucose residue to an acceptor protein. The resulting glucosylated 38-kilodalton polypeptide would then serve as a primer for enzymic glucan chain elongation during the second step. In the present report, we describe the fast protein liquid chromatography purification of UPTG from a membrane pellet of potato tuber. An apparently close association of UPTG, phosphorylase, and starch synthase was observed under native conditions during different purification steps. Enrichment of a 38-kilodalton polypeptide was found throughout enzyme purification. It is now shown that the purified UPTG, with an apparent molecular mass of 38 kilodaltons, undergoes self-glucosylation in a UDP-glucose- and Mn2+-dependent reaction. Therefore, it is concluded that UPTG is the enzyme and at the same time the priming protein required for the biogenesis of protein-bound α-glucan in potato tuber.
format	Artículo Artículo publishedVersion
author	Ardila, F.J. Tandecarz, J.S.
author_facet	Ardila, F.J. Tandecarz, J.S.
author_sort	Ardila, F.J.
title	Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
title_short	Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
title_full	Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
title_fullStr	Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
title_full_unstemmed	Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
title_sort	potato tuber udp-glucose: protein transglucosylase catalyzes its own glucosylation
publishDate	1992
url	http://hdl.handle.net/20.500.12110/paper_00320889_v99_n4_p1342_Ardila http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00320889_v99_n4_p1342_Ardila_oai
work_keys_str_mv	AT ardilafj potatotuberudpglucoseproteintransglucosylasecatalyzesitsownglucosylation AT tandecarzjs potatotuberudpglucoseproteintransglucosylasecatalyzesitsownglucosylation
_version_	1766026627525902336

Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation

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