Structure of the novel monomeric glyoxalase I from Zea mays

TURRA GL; AGOSTINI RB; FAUGUEL CM; PRESELLO DANIEL; ANDREO CS; GONZALEZ JM; CAMPOS BERMUDEZ VA

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 2015 vol. 71 p. 2009 - 2020

0907-4449

The glyoxalase system is ubiquitous among all forms of life owing to its centralrole in relieving the cell from the accumulation of methylglyoxal, a toxicmetabolic byproduct. In higher plants, this system is upregulated under diversemetabolic stress conditions, such as in the defence response to infection bypathogenic microorganisms. Despite their proven fundamental role in metabolicstresses, plant glyoxalases have been poorly studied. In this work, glyoxalase Ifrom Zea mays has been characterized both biochemically and structurally, thusreporting the first atomic model of a glyoxalase I available from plants. Theresults 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.