Structure of the novel monomeric glyoxalase I from Zea mays
The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to...
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| Format: | info:ar-repo/semantics/artículo |
| Language: | Inglés |
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International Union of Crystallography
2019
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| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S1399004715015205 http://hdl.handle.net/20.500.12123/5011 https://doi.org/10.1107/S1399004715015205 |
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| author | Turra, Gino L. Agostini, Romina Belén Fauguel, Carolina Maria Presello, Daniel Alberto Andreo, Carlos Santiago Gonzalez, Javier M. Campos Bermudez, Valeria Alina |
| author_browse | Agostini, Romina Belén Andreo, Carlos Santiago Campos Bermudez, Valeria Alina Fauguel, Carolina Maria Gonzalez, Javier M. Presello, Daniel Alberto Turra, Gino L. |
| author_facet | Turra, Gino L. Agostini, Romina Belén Fauguel, Carolina Maria Presello, Daniel Alberto Andreo, Carlos Santiago Gonzalez, Javier M. Campos Bermudez, Valeria Alina |
| author_sort | Turra, Gino L. |
| collection | INTA Digital |
| description | The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to infection by pathogenic microorganisms. Despite their proven fundamental role in metabolic stresses, plant glyoxalases have been poorly studied. In this work, glyoxalase I from Zea mays has been characterized both biochemically and structurally, thus reporting the first atomic model of a glyoxalase I available from plants. The results indicate that this enzyme comprises a single polypeptide with two structurally similar domains, giving rise to two lateral concavities, one of which harbours a functional nickel(II)-binding active site. The putative function of the remaining cryptic active site remains to be determined. |
| format | info:ar-repo/semantics/artículo |
| id | INTA5011 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2019 |
| publishDateRange | 2019 |
| publishDateSort | 2019 |
| publisher | International Union of Crystallography |
| publisherStr | International Union of Crystallography |
| record_format | dspace |
| spelling | INTA50112019-04-30T12:26:53Z Structure of the novel monomeric glyoxalase I from Zea mays Turra, Gino L. Agostini, Romina Belén Fauguel, Carolina Maria Presello, Daniel Alberto Andreo, Carlos Santiago Gonzalez, Javier M. Campos Bermudez, Valeria Alina Maíz Enzimas Maize Enzymes Glyoxalasa Estrés Metabólico Glyoxalase Methylglyoxal The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to infection by pathogenic microorganisms. Despite their proven fundamental role in metabolic stresses, plant glyoxalases have been poorly studied. In this work, glyoxalase I from Zea mays has been characterized both biochemically and structurally, thus reporting the first atomic model of a glyoxalase I available from plants. The results indicate that this enzyme comprises a single polypeptide with two structurally similar domains, giving rise to two lateral concavities, one of which harbours a functional nickel(II)-binding active site. The putative function of the remaining cryptic active site remains to be determined. EEA Pergamino Fil: Turra, Gino L. 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; Argentina Fil: 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; Argentina Fil: Fauguel, Carolina Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina Fil: Presello, Daniel Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina Fil: 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; Argentina Fil: Gonzalez, Javier M. Los Alamos National Laboratory. Bioscience Division. Protein Crystallography Station; Estados Unidos Fil: 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; Argentina 2019-04-30T12:23:50Z 2019-04-30T12:23:50Z 2015-10 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://scripts.iucr.org/cgi-bin/paper?S1399004715015205 http://hdl.handle.net/20.500.12123/5011 2059-7983 https://doi.org/10.1107/S1399004715015205 eng info:eu-repo/semantics/restrictedAccess application/pdf International Union of Crystallography Acta Crystallographica Section D-Biological Crystallography 71 (Part 10) : 2009-2020 (October 2015) |
| spellingShingle | Maíz Enzimas Maize Enzymes Glyoxalasa Estrés Metabólico Glyoxalase Methylglyoxal Turra, Gino L. Agostini, Romina Belén Fauguel, Carolina Maria Presello, Daniel Alberto Andreo, Carlos Santiago Gonzalez, Javier M. Campos Bermudez, Valeria Alina Structure of the novel monomeric glyoxalase I from Zea mays |
| title | Structure of the novel monomeric glyoxalase I from Zea mays |
| title_full | Structure of the novel monomeric glyoxalase I from Zea mays |
| title_fullStr | Structure of the novel monomeric glyoxalase I from Zea mays |
| title_full_unstemmed | Structure of the novel monomeric glyoxalase I from Zea mays |
| title_short | Structure of the novel monomeric glyoxalase I from Zea mays |
| title_sort | structure of the novel monomeric glyoxalase i from zea mays |
| topic | Maíz Enzimas Maize Enzymes Glyoxalasa Estrés Metabólico Glyoxalase Methylglyoxal |
| url | http://scripts.iucr.org/cgi-bin/paper?S1399004715015205 http://hdl.handle.net/20.500.12123/5011 https://doi.org/10.1107/S1399004715015205 |
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