Structure of the novel monomeric glyoxalase I from Zea mays

GINO TURRA; CARLOS ANDREO; JAVIER MARCELO GONZÁLEZ; VALERIA A. CAMPOS-BERMUDEZ

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

WILEY-BLACKWELL PUBLISHING, INC

Año: 2015 vol. D71 p. 2009 - 2020

0907-4449

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 twostructurally similar domains, giving rise to two lateral concavities, one of whichharbours a functional nickel(II)-binding active site. The putative function of theremaining cryptic active site remains to be determined.