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  • factor xa inhibitor Due to the high structural similarity

    2021-10-09

    Due to the high structural similarity between GlxI and FosA, it is possible that GlxI directed evolution experiments could produce FosA enzymatic activity in a GlxI enzyme. Although the current investigation was unable to detect FosA activity by mutation of a key metal liganding residue in the active site of E. coli GlxI, additional studies on the evolution of antibiotic (FosA) and toxic metabolite (Glx) resistance proteins from ancestral protoresistance proteins is a subject of exciting current interest [70] and worthy of further investigation.
    Acknowledgments The authors would like to thank Dr. Richard Smith for electrospray ionization mass spectrometry analysis of the samples and Dr. Zhengding Su for sharing his knowledge and suggestions. This research was supported by the Natural Sciences and Engineering Research Council of Canada (NSERC) (JFH), University of Waterloo (Ontario, Canada), an NSERC graduate scholarship (to NS), the Government of Thailand (graduate scholarship to US) and the Government of China (visiting scientist award to YR). The funding sources had no involvement in any of the aspects of the experimental research, the interpretation of results or the preparation of this article.
    Methylglyoxal (MG) is a transition-state intermediate of both the triose-phosphates (dihydroxyacetone phosphate and glyceraldehyde-3-phosphate) of glycolysis pathway in eukaryotic factor xa inhibitor . It can also accumulate inside the cells by the leakage of 1,2-enediolate intermediate from the active site of triose phosphate isomerase . Moreover, MG can also be synthesized through the action of MG synthase . Higher level accumulation of MG is toxic to the cell as it inhibits cell proliferation and results in a number of adverse effects such as increasing the degradation of proteins by modifying Arg, Lys, and Cys residues, adducting with guanyl nucleotide in DNA, and inactivating antioxidant defense system . Glyoxalase system comprises of two enzymes, glyoxalase I (gly I) and glyoxalase II (gly II), which catalyze the detoxification of MG to -lactate using reduced glutathione (GSH) as the cofactor and in the process GSH is recycled back , . The reaction catalyzed by gly I and gly II is as follows: Glyoxalase enzymes have been extensively studied in microbial and animal systems , . The existence and widespread distribution of this shunt pathway indicate its universal role in primary metabolism , . Though very little work has been done in plants, differences in the pattern of enzyme distribution have been shown in Douglas-fir needles and their callus due to the presence and absence of MG, respectively , and the biological significance of this pathway under stress is just beginning to be explored , , . Role of glyoxalases under stress in humans due to exercise, or in animals after irradiation or glycerol load in bacteria has been indicated . However, recent studies in plants have demonstrated that different kind of stress conditions, such as salt and metal stress, results in enhanced expression of . Transgenic tobacco plants overexpressing and genes individually or together in the same plant indicated their role in salt tolerance . However, whether or not MG accumulates in plants in response to stress conditions remains to be addressed. Recently, it has been shown that MG can also act as a signal molecule and hence its levels need to be regulated. MG levels have been measured in animal and yeast systems , . However, there are no reports on the estimation of MG in plants. The isolation, purification, and characterization of various enzymes, involved in the biosynthesis and breakdown of MG, has previously been reported in animals , . In the present study, we have standardized the protocol for the estimation of MG in plants and document that MG levels increase significantly in plants in response to salinity, drought, and cold stress conditions. Its levels were regulated by gly I and glutathione levels under normal and salt stress conditions.