Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays

Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxa...

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Detalhes bibliográficos
Autores: Gonzalez, Javier Marcelo, Agostini, Romina Belén, Alvarez, Clarisa Ester, Klinke, Sebastian, Andreo, Carlos Santiago, Campos Bermudez, Valeria Alina
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/151610
Acesso em linha:http://hdl.handle.net/11336/151610
Access Level:acceso abierto
Palavra-chave:GLYOXALASE I
HEMITHIOACETAL
MAIZE
METHYLGLYOXAL
PROTEIN TUNNEL
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
id AR_ed5cbbfa88deeaf97f666b9ab4e3c953
oai_identifier_str oai:ri.conicet.gov.ar:11336/151610
network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
title Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
spellingShingle Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
Gonzalez, Javier Marcelo
GLYOXALASE I
HEMITHIOACETAL
MAIZE
METHYLGLYOXAL
PROTEIN TUNNEL
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
title_full Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
title_fullStr Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
title_full_unstemmed Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
title_sort Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
dc.creator.none.fl_str_mv Gonzalez, Javier Marcelo
Agostini, Romina Belén
Alvarez, Clarisa Ester
Klinke, Sebastian
Andreo, Carlos Santiago
Campos Bermudez, Valeria Alina
author Gonzalez, Javier Marcelo
author_facet Gonzalez, Javier Marcelo
Agostini, Romina Belén
Alvarez, Clarisa Ester
Klinke, Sebastian
Andreo, Carlos Santiago
Campos Bermudez, Valeria Alina
author_role author
author2 Agostini, Romina Belén
Alvarez, Clarisa Ester
Klinke, Sebastian
Andreo, Carlos Santiago
Campos Bermudez, Valeria Alina
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv GLYOXALASE I
HEMITHIOACETAL
MAIZE
METHYLGLYOXAL
PROTEIN TUNNEL
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic GLYOXALASE I
HEMITHIOACETAL
MAIZE
METHYLGLYOXAL
PROTEIN TUNNEL
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxalase I from maize exhibits a symmetric fold with two cavities, potentially harboring two active sites, in analogy with homodimeric enzyme surrogates. Here we confirm that only one of the two cavities exhibits glyoxalase I activity and show that it adopts a tunnel-shaped structure upon substrate binding. Such conformational change gives rise to independent binding sites for glutathione and methylglyoxal in the same active site, with important implications for the molecular reaction mechanism, which has been a matter of debate for several decades. Database: Structural data are available in The Protein Data Bank database under the accession numbers 6BNN, 6BNX, and 6BNZ.
publishDate 2019
dc.date.none.fl_str_mv 2019-08
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/11336/151610
Gonzalez, Javier Marcelo; Agostini, Romina Belén; Alvarez, Clarisa Ester; Klinke, Sebastian; Andreo, Carlos Santiago; et al.; Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays; Wiley Blackwell Publishing, Inc; Febs Journal; 286; 16; 8-2019; 3255-3271
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/151610
identifier_str_mv Gonzalez, Javier Marcelo; Agostini, Romina Belén; Alvarez, Clarisa Ester; Klinke, Sebastian; Andreo, Carlos Santiago; et al.; Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays; Wiley Blackwell Publishing, Inc; Febs Journal; 286; 16; 8-2019; 3255-3271
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/febs.14855
info:eu-repo/semantics/altIdentifier/doi/10.1111/febs.14855
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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
_version_ 1799194969115721728
spelling Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea maysGonzalez, Javier MarceloAgostini, Romina BelénAlvarez, Clarisa EsterKlinke, SebastianAndreo, Carlos SantiagoCampos Bermudez, Valeria AlinaGLYOXALASE IHEMITHIOACETALMAIZEMETHYLGLYOXALPROTEIN TUNNELhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione hemithioacetal intermediate. Recently, we have shown that the monomeric glyoxalase I from maize exhibits a symmetric fold with two cavities, potentially harboring two active sites, in analogy with homodimeric enzyme surrogates. Here we confirm that only one of the two cavities exhibits glyoxalase I activity and show that it adopts a tunnel-shaped structure upon substrate binding. Such conformational change gives rise to independent binding sites for glutathione and methylglyoxal in the same active site, with important implications for the molecular reaction mechanism, which has been a matter of debate for several decades. Database: Structural data are available in The Protein Data Bank database under the accession numbers 6BNN, 6BNX, and 6BNZ.Fil: Gonzalez, Javier Marcelo. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Agostini, Romina Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Campos Bermudez, Valeria Alina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaWiley Blackwell Publishing, Inc2019-08info: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/11336/151610Gonzalez, Javier Marcelo; Agostini, Romina Belén; Alvarez, Clarisa Ester; Klinke, Sebastian; Andreo, Carlos Santiago; et al.; Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays; Wiley Blackwell Publishing, Inc; Febs Journal; 286; 16; 8-2019; 3255-32711742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/febs.14855info:eu-repo/semantics/altIdentifier/doi/10.1111/febs.14855info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:40:17Zoai:ri.conicet.gov.ar:11336/151610instacron: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:34982024-05-08 13:40:17.54CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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