Structure of the novel monomeric glyoxalase I fromZea mays

Abstract

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.

Genome-wide analysis and expression profiling of glyoxalase gene families in soybean (Glycine max) indicate their development and abiotic stress specific response

“…To know the arrangement of active site residues and overall 3-D coordination, homology model of GmGLYI-3, GmGLYI-16 and GmGLYII-5 proteins was built (Fig. 8 ) based on the closely related template structure of Zea mays GLYI (PDB: 5D7Z) [ 43 ], mouse GLYI (PDB: 4OPN), and AtGLYII-2 (PDB: 2Q42) [ 30 ] proteins, respectively. GmGLYI-3 is a Ni 2+ -dependent monomeric GLYI enzyme (Fig.…”

Comparative analysis of glyoxalase pathway genes in Erianthus arundinaceus and commercial sugarcane hybrid under salinity and drought conditions

“…Predicted three-dimensional structure of E. arundinaceus and commercial sugarcane hybrid glyoxalase proteins were almost similar. Crystallographic structure of glyoxalase I depicts homodimeric form with each monomer harbouring two structurally similar domains of βαβββ with two active sites [29]. However, monomeric forms of glyoxalase I with four βαβββ were suggested in rice.…”

Dissecting the Physiological Function of Plant Glyoxalase I and Glyoxalase I-Like Proteins

“…In contrast, the two Ni 2+ -dependent GLXI;1 and GLXI;2 are two-domain (domain A and B) VOC proteins of 33 kDa. While these two-domain Ni 2+ -dependent GLXI fold and function as a monomer, the one-domain GLXI;3 and GLXI-like proteins are likely to assemble as homodimers to reconstitute the VOC fold by domain swapping ( He and Moran, 2011 ; Turra et al, 2015 ). Multiple sequence alignments (MSA) as well as comparison of conserved GLXI binding sites revealed essential differences in amino acid (aa) composition among the 11 VOC superfamily members.…”