Cytochromes P450 in Nanodiscs
β Scribed by Ilia G. Denisov; Stephen G. Sligar
- Publisher
- Elsevier Science
- Year
- 2011
- Tongue
- English
- Weight
- 507 KB
- Volume
- 1814
- Category
- Article
- ISSN
- 1570-9639
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Significant changes in drugβmetabolizing enzyme (DME) expression occur during ontogeny. Such changes can have a profound effect on therapeutic efficacy in the fetus and child, as well as the risk for adverse drug reactions. To gain a better understanding of DME ontogeny, enzyme contents
## Abstract Recently, cytochrome P450 170A1 (CYP170A1) has been found to be a bifunctional protein, which catalyzes both monooxygenase activity and terpene synthase activity by two distinct active sites in the wellβestablished P450 protein structure. Therefore, CYP170A1 is identified clearly as a m
## Abstract To maximize redox coupling efficiency with recombinant cytochrome P450 hydroxylases from yew (__Taxus__) species installed in yeast for the production of the anticancer drug Taxol, a cDNA encoding NADPH:cytochrome P450 reductase from __T. cuspidata__ was isolated. This singleβcopy gene
## Abstract Cytochrome __b__~5~, a 17βkDa hemeprotein associated primarily with the endoplasmic reticulum of eukaryotic cells, has long been known to augment some cytochrome P450 monooxygenase reactions, but the mechanism of stimulation has remained controversial. Studies in recent years have clari