Purification and characterization of glyoxalase I from Pseudomonas putida.
Glyoxalase I was purified to apparent homogeneity from Pseudomonas putida. The enzyme was a monomer with a molecular weight of 20,000. The enzyme was most active at pH 8.0. The Km values for methylglyoxal and 4,5-dioxovale-rate are 3.5 mM and 1.2 mM, respectively. Contrary to the case of eukaryotic enzymes, chelating agents showed little inhibitory effects on the enzyme activity. Among the metal ions tested, Zn++ specifically and completely inhibited the activity of the enzyme at a millimolar level. The properties of bacterial glyoxalase I were quite different from mammalian and yeast enzymes.
D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D008190:Lyases / Q000302:isolation & purification*; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D015032:Zinc / Q000494:pharmacology
D004492:Edetic Acid; D008190:Lyases; D007791:Lactoylglutathione Lyase; D015032:Zinc