Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase

Autores
Adachi, Osao; Hours, Roque Alberto; Akakabe, Yoshihiko; Shinagawa, Emiko; Ano, Yoshitaka; Yakushi, Toshiharu; Matsushita, Kazunobu
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
D-Ribose and 2-deoxy-D-ribose were oxidized to 4- keto-D-ribonate and 2-deoxy-4-keto-D-ribonate respectively by oxidative fermentation, and the chemical structures of the oxidation products were confirmed to be as expected. Both pentoses are important sugar components of nucleic acids. When examined, purine nucleosidase activity predominated in the membrane fraction of acetic acid bacteria. This is perhaps the first finding of membrane-bound purine nucleosidase.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Biología
2-deoxy-D-ribose oxidation
D-ribose oxidation
Nucleosidase
Purine-20-deoxyribonucleosidease
Purine-ribonucleosidase
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/85538
Acceder
id SEDICI_258437823db802128e55a56dcf80e606
oai_identifier_str oai:sedici.unlp.edu.ar:10915/85538
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidaseAdachi, OsaoHours, Roque AlbertoAkakabe, YoshihikoShinagawa, EmikoAno, YoshitakaYakushi, ToshiharuMatsushita, KazunobuBiología2-deoxy-D-ribose oxidationD-ribose oxidationNucleosidasePurine-20-deoxyribonucleosideasePurine-ribonucleosidaseD-Ribose and 2-deoxy-D-ribose were oxidized to 4- keto-D-ribonate and 2-deoxy-4-keto-D-ribonate respectively by oxidative fermentation, and the chemical structures of the oxidation products were confirmed to be as expected. Both pentoses are important sugar components of nucleic acids. When examined, purine nucleosidase activity predominated in the membrane fraction of acetic acid bacteria. This is perhaps the first finding of membrane-bound purine nucleosidase.Centro de Investigación y Desarrollo en Fermentaciones Industriales2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1131-1133http://sedici.unlp.edu.ar/handle/10915/85538enginfo:eu-repo/semantics/altIdentifier/issn/0916-8451info:eu-repo/semantics/altIdentifier/doi/10.1271/bbb.130066info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:48:46Zoai:sedici.unlp.edu.ar:10915/85538Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:48:47.119SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
title Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
spellingShingle Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
Adachi, Osao
Biología
2-deoxy-D-ribose oxidation
D-ribose oxidation
Nucleosidase
Purine-20-deoxyribonucleosidease
Purine-ribonucleosidase
title_short Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
title_full Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
title_fullStr Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
title_full_unstemmed Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
title_sort Pentose oxidation by acetic acid bacteria led to a finding of membrane-bound purine nucleosidase
dc.creator.none.fl_str_mv Adachi, Osao
Hours, Roque Alberto
Akakabe, Yoshihiko
Shinagawa, Emiko
Ano, Yoshitaka
Yakushi, Toshiharu
Matsushita, Kazunobu
author Adachi, Osao
author_facet Adachi, Osao
Hours, Roque Alberto
Akakabe, Yoshihiko
Shinagawa, Emiko
Ano, Yoshitaka
Yakushi, Toshiharu
Matsushita, Kazunobu
author_role author
author2 Hours, Roque Alberto
Akakabe, Yoshihiko
Shinagawa, Emiko
Ano, Yoshitaka
Yakushi, Toshiharu
Matsushita, Kazunobu
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Biología
2-deoxy-D-ribose oxidation
D-ribose oxidation
Nucleosidase
Purine-20-deoxyribonucleosidease
Purine-ribonucleosidase
topic Biología
2-deoxy-D-ribose oxidation
D-ribose oxidation
Nucleosidase
Purine-20-deoxyribonucleosidease
Purine-ribonucleosidase
dc.description.none.fl_txt_mv D-Ribose and 2-deoxy-D-ribose were oxidized to 4- keto-D-ribonate and 2-deoxy-4-keto-D-ribonate respectively by oxidative fermentation, and the chemical structures of the oxidation products were confirmed to be as expected. Both pentoses are important sugar components of nucleic acids. When examined, purine nucleosidase activity predominated in the membrane fraction of acetic acid bacteria. This is perhaps the first finding of membrane-bound purine nucleosidase.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description D-Ribose and 2-deoxy-D-ribose were oxidized to 4- keto-D-ribonate and 2-deoxy-4-keto-D-ribonate respectively by oxidative fermentation, and the chemical structures of the oxidation products were confirmed to be as expected. Both pentoses are important sugar components of nucleic acids. When examined, purine nucleosidase activity predominated in the membrane fraction of acetic acid bacteria. This is perhaps the first finding of membrane-bound purine nucleosidase.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/85538
url http://sedici.unlp.edu.ar/handle/10915/85538
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0916-8451
info:eu-repo/semantics/altIdentifier/doi/10.1271/bbb.130066
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1131-1133
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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