The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418

Autores
Buurman, Ed T.; Boiardi, José Luis; Teixeira de Mattos, M. Joost; Neijssel, Oense M.
Año de publicación
1990
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Magnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 μM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the glucose dehydrogenase (GDH) activities also increased and became similar to those observed in potassium- or phosphate limited cultures. It is concluded that this is due to Mg2+ and Ca2+ ions being involved in the binding of pyrroloquinoline quinone (PQQ) to the GDH apoenzyme. There seems to be an absolute requirement of divalent cations for proper enzyme functioning and in this respect Ca2+ ions could replace Mg2+ ions. The high GDH activity which has been found in cells grown under Mg2−-limited conditions in the presence of higher concentrations of Ca2+ ions, is compatible with the earlier proposal that GDH functions as an auxiliary energy generating system involved in the maintenance of high transmembrane ion gradients.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Química
Klebsiella pneumoniae
Chemostat culture
Glucose metabolism
Glucose dehydrogenase
Pyrroloquinoline quinone
Magnesium
Calcium
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:10915/138545
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/138545
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418Buurman, Ed T.Boiardi, José LuisTeixeira de Mattos, M. JoostNeijssel, Oense M.QuímicaKlebsiella pneumoniaeChemostat cultureGlucose metabolismGlucose dehydrogenasePyrroloquinoline quinoneMagnesiumCalciumMagnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 μM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the glucose dehydrogenase (GDH) activities also increased and became similar to those observed in potassium- or phosphate limited cultures. It is concluded that this is due to Mg2+ and Ca2+ ions being involved in the binding of pyrroloquinoline quinone (PQQ) to the GDH apoenzyme. There seems to be an absolute requirement of divalent cations for proper enzyme functioning and in this respect Ca2+ ions could replace Mg2+ ions. The high GDH activity which has been found in cells grown under Mg2−-limited conditions in the presence of higher concentrations of Ca2+ ions, is compatible with the earlier proposal that GDH functions as an auxiliary energy generating system involved in the maintenance of high transmembrane ion gradients.Centro de Investigación y Desarrollo en Fermentaciones Industriales1990info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf502-505http://sedici.unlp.edu.ar/handle/10915/138545enginfo:eu-repo/semantics/altIdentifier/issn/0302-8933info:eu-repo/semantics/altIdentifier/issn/1432-072Xinfo:eu-repo/semantics/altIdentifier/doi/10.1007/bf00248434info:eu-repo/semantics/altIdentifier/pmid/2160228info: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:UNLP2025-09-29T11:31:57Zoai:sedici.unlp.edu.ar:10915/138545Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:31:58.236SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
title The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
spellingShingle The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
Buurman, Ed T.
Química
Klebsiella pneumoniae
Chemostat culture
Glucose metabolism
Glucose dehydrogenase
Pyrroloquinoline quinone
Magnesium
Calcium
title_short The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
title_full The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
title_fullStr The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
title_full_unstemmed The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
title_sort The role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
dc.creator.none.fl_str_mv Buurman, Ed T.
Boiardi, José Luis
Teixeira de Mattos, M. Joost
Neijssel, Oense M.
author Buurman, Ed T.
author_facet Buurman, Ed T.
Boiardi, José Luis
Teixeira de Mattos, M. Joost
Neijssel, Oense M.
author_role author
author2 Boiardi, José Luis
Teixeira de Mattos, M. Joost
Neijssel, Oense M.
author2_role author
author
author
dc.subject.none.fl_str_mv Química
Klebsiella pneumoniae
Chemostat culture
Glucose metabolism
Glucose dehydrogenase
Pyrroloquinoline quinone
Magnesium
Calcium
topic Química
Klebsiella pneumoniae
Chemostat culture
Glucose metabolism
Glucose dehydrogenase
Pyrroloquinoline quinone
Magnesium
Calcium
dc.description.none.fl_txt_mv Magnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 μM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the glucose dehydrogenase (GDH) activities also increased and became similar to those observed in potassium- or phosphate limited cultures. It is concluded that this is due to Mg2+ and Ca2+ ions being involved in the binding of pyrroloquinoline quinone (PQQ) to the GDH apoenzyme. There seems to be an absolute requirement of divalent cations for proper enzyme functioning and in this respect Ca2+ ions could replace Mg2+ ions. The high GDH activity which has been found in cells grown under Mg2−-limited conditions in the presence of higher concentrations of Ca2+ ions, is compatible with the earlier proposal that GDH functions as an auxiliary energy generating system involved in the maintenance of high transmembrane ion gradients.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description Magnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 μM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the glucose dehydrogenase (GDH) activities also increased and became similar to those observed in potassium- or phosphate limited cultures. It is concluded that this is due to Mg2+ and Ca2+ ions being involved in the binding of pyrroloquinoline quinone (PQQ) to the GDH apoenzyme. There seems to be an absolute requirement of divalent cations for proper enzyme functioning and in this respect Ca2+ ions could replace Mg2+ ions. The high GDH activity which has been found in cells grown under Mg2−-limited conditions in the presence of higher concentrations of Ca2+ ions, is compatible with the earlier proposal that GDH functions as an auxiliary energy generating system involved in the maintenance of high transmembrane ion gradients.
publishDate 1990
dc.date.none.fl_str_mv 1990
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/10915/138545
url http://sedici.unlp.edu.ar/handle/10915/138545
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0302-8933
info:eu-repo/semantics/altIdentifier/issn/1432-072X
info:eu-repo/semantics/altIdentifier/doi/10.1007/bf00248434
info:eu-repo/semantics/altIdentifier/pmid/2160228
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
502-505
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 13.070432

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