Bacterial glyoxalase enzymes

The glyoxalase system is composed of two metalloenzymes, Glyoxalase I and Glyoxalase II. This system is important in the detoxification of methylglyoxal, among other roles. Detailed studies have determined that a number of bacterial Glyoxalase I enzymes are maximally activated by Ni2+ and Co2+ ions, but are inactive in the presence of Zn2+. This is in contrast to the Glyoxalase I enzyme from humans, which is catalytically active with Zn2+ as well as a number of other metal ions. The structure-activity relationships between these two classes of Glyoxalase I are serving as important clues to how the molecular structures of these proteins control metal activation profiles as well as to clarify the mechanistic chemistry of these catalysts. In addition, the possibility of targeting inhibitors against the bacterial versus human enzyme has the potential to lead to new approaches to combat bacterial infections.