Publisher Summary The chapter discusses the biologically relevant chemistry of glutathione (GSH) and its occurrence in microbial cells The GSH-related biochemical reactions and the physiological roles of GSH are summarized The biosynthesis of GSH is remarkable in two ways: it is mRNA independent, and the glutamic residue is joined in an unusual peptide linkage of the γ -carbon atom to the cysteine residue Due to this structural peculiarity, GSH is protected against proteolytic cleavage The GSH status of cells is defined by the total concentration of GSH and the nature and distribution of the possible forms of occurrence of the tripeptide in the cell GSH and related compounds are widespread in the microbial world, especially amongst organisms with an aerobic lifestyle This observation emphasizes the role of GSH in cellular protection against by-products generated by oxidative metabolism, but it does not limit its functions to this role Glutathione acts as an enzyme cofactor, transport component, nucleophilic substrate, and sulphur reservoir; and participates in key cellular processes such as protein synthesis and degradation, regulation of enzyme activity, synthesis of DNA, and maintenance of the integrity of cell membranes and organelles Having a functional diversity, GSH is interrelated with a number of metabolic pathways and its intracellular modulation could have an impact on the entire cell, making it extremely difficult to associate directly a given cellular end-point with one molecule or system Both in Escherichia coli and Saccharomyces cerevisiae, GSH plays an important role in cellular protection during chemical stresses in spite of the fact that key enzymes of detoxification, such as GSH peroxidase and GSH S-transferase, remain at a low level

Metabolism and functions of glutathione in micro-organisms.

A new paradigm for biohydroxylation by Beauveria bassiana ATCC 7159

Cell extracts of the filamentous fungus Cunninghamella elegans contain epoxide hydrolase (EC 3.3.2.3), glutathione S-transferase (EC 2.5.1.18) and UDP-glucuronosyltransferase (EC 2.4.1.17) activities. Epoxide hydrolase activity was determined with p-nitrostyrene oxide as substrate and was shown to be associated with the 100 000 g pellet obtained from disrupted mycelia. Glutathione S-transferase activity was demonstrated with 1-chloro-2,4-dinitrobenzene and p-nitrobenzyl chloride as substrates. The presence of two or more glutathione S-transferase activities was indicated by different activity ratios for the two substrates in different extracts, and by distinct thermal denaturation curves. UDP-glucuronosyltransferase activity with 3-hydroxybenzo[a]pyrene as substrate was found only with the non-sedimentable fraction prepared from ruptured mycelia.

Metabolism ofxenobiotic compounds byenzymes incell extracts ofthe fungus Cunninghamella elegans

The level of glutathione S-transferase (GSH0ST) activity was determined in growing cultures and in washed resting cells of Beauveria strains with and without addition of isosorbide dinitrate (ISDN), by following the reaction with o-dinitrobenzene (o-DNB). The level of GSH-ST varied according to the pH changes of the medium and decreased during culture. The enzymatic activity measured with o-DNB did not correlate with ISDN bioconversion carried out either with B. sulfurescens or B. tenella. Immediately after starting incubation of the resting cells with ISDN, the level of GSH-ST activity initially increased, but declined afterwards, whereas the bioconversion process continued and reached 500 mg/l isosorbide 5-mononitrate. When 1-chloro-2,4-dinitrobenzene was used as a substrate for the evaluation of GSH-ST activity using B. tenella, a conjugation product having a UV absorption at 410 nm was formed.

Isosorbide dinitrate bioconversion by Beauveria strains: implication of glutathione transferase levels

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Isosorbide dinitrate bioconversion by Beauveria strains: implication of glutathione transferase levels