Characterization of human FMO3 and FMO5 expressed as maltose binding protein fusions
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Human kidney flavin-containing monooxygenases and their potential roles in cysteine s-conjugate metabolism and nephrotoxicity.
The potential roles of human hepatic and renal flavin-containing monooxygenases (FMOs) in the metabolism of the cysteine S-conjugates S-allyl cysteine (SAC) and S-(1,2-dichlorovinyl)-L-cysteine (DCVC) were investigated. Incubations of human cDNA-expressed FMO1, FMO3, FMO4, and FMO5 with SAC resulted in detection of SAC sulfoxide, with FMO3 exhibiting approximately 3-, 4-, and 10-fold higher act...
متن کاملCharacterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions.
To examine the possibility for drug metabolism polymorphism, adult human flavin-containing monooxygenases (form 3) (EC 1.14.13.8) that differ at one amino acid were expressed in Escherichia coli as maltose binding protein fusions. The cDNA that was first reported during the cloning of adult human flavin-containing monooxygenase was designated the wild type lys158 enzyme. A second cDNA has been ...
متن کاملMarmoset Flavin-Containing Monooxygenase 3 in the Liver Is a Major Benzydamine and Sulindac Sulfide Oxygenase.
Common marmosets (Callithrix jacchus) are potentially primate models for preclinical drug metabolism studies because there are similarities in the molecular characteristics of cytochrome P450 enzymes between this species and humans. However, characterization of non-cytochrome P450 enzymes has not been clarified in marmosets. Here, we report characterization of flavin-containing monooxygenases F...
متن کاملAlternative processing events in human FMO genes.
In humans, flavin-containing monooxygenase (FMO) functional diversity is determined by the expression of five FMO genes, named FMO1 to FMO5, and their variants. In this study, we systematically analyzed transcripts of FMO1 to FMO5 in different human tissues by reverse-transcription-polymerase chain reaction and identified a large number of splice variants. Exon skipping was the major splicing e...
متن کاملHeterologous Expression of Mycobacterial Esx Complexes in Escherichia coli for Structural Studies Is Facilitated by the Use of Maltose Binding Protein Fusions
The expression of heteroligomeric protein complexes for structural studies often requires a special coexpression strategy. The reason is that the solubility and proper folding of each subunit of the complex requires physical association with other subunits of the complex. The genomes of pathogenic mycobacteria encode many small protein complexes, implicated in bacterial fitness and pathogenicit...
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تاریخ انتشار 2010