title: Bacterial glyoxalase I enzymes: structural and biochemical investigations.
abstract: 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.
authors.affiliation: *Department of Chemistry, University of Waterloo, 200 University Avenue West, Waterloo, Ontario, Canada, N2L 3G1.
authors.forename: John F
authors.initials: JF
authors.lastname: Honek
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D007477:Ions / Q000378:metabolism; D007791:Lactoylglutathione Lyase / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D007477:Ions; D007791:Lactoylglutathione Lyase