• Microbiology and Biotechnology Letters
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• v.18 no.1
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• pp.103-108
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• 1990

The enzymatic studies on the methylglyoxal metabolism in yeast and bacterial cells indicated that organisms are equipped with the common and manifold systems for the detoxification of methylglyoxal. Among these systems, the glyoxalase I is the most important route for methylglyoxal detoxification. The molecular structure of glyoxalase I is apparently distinct from the enzyme sources, and zinc ion is an essential cofactor in enzyme activity. The gene for Pseudomonas putida glyoxalase I functioned as a scavenger of methylglyoxal and regulated the cell size of the bacterium. Comparison of the nucleotide sequence of the P. putida glyoxalase I gene with the N-terminal amino acid sequence of the purified enzyme revealed that the N-terminal methionine residue was removed after translation. Possible physiological role of glyoxalase I was also discussed.