Disease relevance of GLX2-2

• Within this protein family, glyoxalase II from Arabidopsis thaliana is the first member to be isolated with significant amounts of iron, manganese, and zinc when being recombinantly produced in Escherichia coli [1].

High impact information on GLX2-2

• Information presented here provides new insights into the active site and reaction mechanism of glyoxalase II that can be used for the rational design of glyoxalase II inhibitors [2].
• Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo [1].
• Homogeneous enzyme was obtained by affinity purification and its catalytic parameters with thiolesters of glutathione were similar to those for human glyoxalase II [3].
• Searches in databanks identified seven additional DNA sequences from different species with high similarity to glyoxalase II [3].
• The enzymes produced in minimal media were active towards the substrate S-D-lactoylglutathione, yielding kcat/ Km values similar to those of rich media GLX2-2 [4].

Biological context of GLX2-2

• Southern blot and sequence analyses indicate that glyoxalase II proteins are encoded by at least two multigene families in Arabidopsis [5].
• Because of its role in chemical detoxification, glyoxalase II has been studied as a potential anti-cancer and/or anti-protozoal target; however, very little is known about the active site and reaction mechanism of this important enzyme [2].
• Glyoxalase II, one of the enzymes of the glyoxalase pathway, cDNA cloned from rice (OsglyII) consists of 1623 nucleotides with an open reading frame of 1010bp encoding a polypeptide of 336 amino acids and an estimated isoelectric point of 8.08 [6].
• The mRNA levels of a diverse array of gene products increases during leaf senescence, including a protease, a ribosomal protein, two cinnamyl alcohol dehydrogenases, a nitrilase and glyoxalase II [7].

Associations of GLX2-2 with chemical compounds

• Glyoxalase II is part of the glutathione-dependent glyoxalase detoxification system [5].
• Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity [8].

Analytical, diagnostic and therapeutic context of GLX2-2

• Molecular cloning and characterization of the thiolesterase glyoxalase II from Arabidopsis thaliana [3].

References