A series of soluble epoxide hydrolase (sEH) inhibitors containing halogenated pyrazoles was developed. Inhibition potency of the obtained compounds ranges from 0.8 to 27.
View Article and Find Full Text PDFGlutathione overproducers were detected by examining the pigmentation intensity of Saccharomyces cerevisiae met30 yeast carrying wild-type alleles for ADE1 and ADE2. Highly pigmented colonies, phenocopies of the ade2 or ade1 mutants, were observed among yeast grown in minimal biotin-free medium with a high methionine content.
View Article and Find Full Text PDFWe identified Saccharomyces cerevisiae mutants with 100% higher intracellular glutathione using 1-methyl-3-nitro-1-nitrosoguanidine mutagenesis. This method employs visual selection of the most pigmented colonies among met30 strains carrying ade1 and ade2 mutations. Since the method does not involve genetic engineering, the mutants are suitable for use in the food industry.
View Article and Find Full Text PDFA collection of spontaneous "Roman's mutants" (1654 mutants) for early genes of purine biosynthesis PUR1-PUR5 was obtained from 16 parental ade1(pur6) and ade2(pur7) strains of the methylotrophic yeast Pichia methanolica. Two genes, bifunctiional ADE7,4(PUR2,5) and ADES(PUR4), were identified earlier. For identification of the two remaining early genes (ADE3 and ADE8), a novel approach was used: a comparison of spectra of spontaneous Roman's mutants and relative sizes of genes (with regard to the length of polypeptides in amino acid residues).
View Article and Find Full Text PDFTwo independent mutant strains of methylotrophic yeast Pichia methanolica (mth1 arg1 and mth2 arg4) from the initial line 616 (ade1 ade5) were investigated. The mutant strains possessed defects in genes MTH1 and MTH2 which resulted in the inability to assimilate methanol as a sole carbon source and the increased activity of alcohol oxidase (AO). The function of the AUG2 gene encoding one of the subunits of AO and CTA1, a probable homolog of peroxisomal catalase of Saccharomyces cereviseae, was investigated by analyses of the molecular forms of isoenzymes.
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