Recombinant yeast in drug metabolism
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Cited by (45)
Engineering of redox partners and cofactor NADPH supply of CYP68JX for efficient steroid two-step ordered selective hydroxylation activity
2024, Journal of Steroid Biochemistry and Molecular BiologyComparative functional characterization of a novel benzoate hydroxylase cytochrome P450 of Fusarium oxysporum
2015, Enzyme and Microbial TechnologyCitation Excerpt :Upon spectral analysis of the yeast microsomes, it was evident that the eukaryotic gene was able to be well expressed in the active form without any gene modifications, and hence we proceeded to characterize the catalytic properties of FoCYP53A19 in the yeast system. The cytochrome P450 reductase from yeast is an efficient redox donor for transferring electrons to various heterologous eukaryotic CYPs [21–23]. To compare the significance of CPR over the catalytic efficiency of FoCYP53A19, the well reported yeast NADPH reductases from S. cerevisiae (ScCPR) and C. albicans (CaCPR) were employed [21,24].
Metabolism related toxicity of diclofenac in yeast as model system
2011, Toxicology LettersCitation Excerpt :Advantages of yeast over mammalian cell systems are its easy manipulation, cost-effectiveness, and rapid growth. Because wild type yeast strains lack drug-metabolizing cytochrome P450s and glucuronosyl-transferases, many biotransformation enzymes have been heterologously expressed in yeast (Pompon et al., 1997; Renaud et al., 1993). Expression of mammalian P450s in yeast has been used to investigate the mutagenic effects of oxidative metabolites of xenobiotics, as has been described for N-alkylformamides and aflatoxine B1 (Del Carratore et al., 2000; Guo et al., 2005).
Organic transformations catalyzed by engineered yeast cells and related systems
2000, Current Opinion in Biotechnology