1. Converting GLX2-1 into an active glyoxalase II
- Author
-
Limphong, Pattraranee, Adams, Nicole E., Rouhier, Matthew F., McKinney, Ross M., Naylor, Melissa, Bennett, Brian, Makaroff, Christopher A., and Crowder, Michael W.
- Subjects
Arabidopsis thaliana -- Genetic aspects ,Arabidopsis thaliana -- Physiological aspects ,Enzyme binding -- Analysis ,Gene expression -- Analysis ,Tyrosine -- Chemical properties ,Biological sciences ,Chemistry - Abstract
The enzymes obtained from the alteration of amino acids residues at positions 219, 246, 248, 325, and 328 in Arabidopsis thaliana glyoxalase 2-1 (GLX2-1) were overexpressed, purified, and characterized to identify residues essential for GLX2 substrate activity. The results revealed that an active GLX2 enzyme requires both the presence of a properly positioned metal center and significant nonmetal, enzyme-substrate contacts, with the most important tyrosine 255.
- Published
- 2010