A number of bacterial glyoxalase I enzymes are maximally activated by Ni2+ and Co2+ ions, but are inactive in the presence of Zn2+, yet these enzymes will also bind this metal ion. The structure–activity relationships between these two classes of glyoxalase I serve as important clues as to how the molecular structures of these proteins control metal-activation profiles.

Keywords:
Clostridium acetobutylicum, Escherichia coli, glyoxalase, metal activation, metalloenzyme, protein structure
© The Authors Journal compilation © 2014 Biochemical Society
2014
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