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Structure of the novel monomeric glyoxalase I from Zea mays
Resumen
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,
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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.
[Cerrar]
Autor
Turra, Gino L.;
Agostini, Romina Belén;
Fauguel, Carolina Maria;
Presello, Daniel Alberto;
Andreo, Carlos Santiago;
Gonzalez, Javier M.;
Campos Bermudez, Valeria Alina;
Fuente
Acta Crystallographica Section D-Biological Crystallography 71 (Part 10) : 2009-2020 (October 2015)
Fecha
2015-10
Editorial
International Union of Crystallography
ISSN
2059-7983
Formato
pdf
Tipo de documento
artículo
Palabras Claves
Derechos de acceso
Restringido
Excepto donde se diga explicitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)