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Mass Spectrometry and Luminogenic-based Approaches to Characterize Phase I Metabolic Competency of In Vitro Cell Cultures
Published on: March 28, 2017
Diversity and substrate specificity in the structures of steroidogenic cytochrome P450 enzymes
Hiroshi Sugimoto1, Yoshitsugu Shiro
1Biometal Science Laboratory, RIKEN SPring Center, Sayo, Hyogo, Japan. sugimoto@spring8.or.jp
Abstract:
Mammalian cytochrome P450 (CYP) comprise a large group of enzymes that play many important roles in the biosynthesis of steroid hormones and vitamins. In addition, they participate in the metabolism of drugs and xenobiotics. All known mammalian CYP enzymes are membrane-associated proteins, which complicated their X-ray crystallographic analysis. In recent years, however, significant progress has been made in the X-ray crystallographic analysis of mammalian CYP enzymes involved in the steroid hormone and vitamin D(3) metabolism. The knowledge from three-dimensional structures of mammalian CYP enzymes will benefit drug discovery and development.
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