Journal
CHEMICAL RESEARCH IN TOXICOLOGY
Volume 27, Issue 9, Pages 1474-1486Publisher
AMER CHEMICAL SOC
DOI: 10.1021/tx500203s
Keywords
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Funding
- National Center for Research Resources [P20-RR021940-07]
- National Institute of General Medical Sciences [P20-GM103549-07]
- Kansas IDeA Network of Biomedical Research Excellence from the National Institutes of Health [QH846868-K-INBRE]
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Through their unique oxidative chemistry, cytochrome P450 monooxygenases (CYPs) catalyze the elimination of most drugs and toxins from the human body. Proteinprotein interactions play a critical role in this process. Historically, the study of CYPprotein interactions has focused on their electron transfer partners and allosteric mediators, cytochrome P450 reductase and cytochrome b5. However, CYPs can bind other proteins that also affect CYP function. Some examples include the progesterone receptor membrane component 1, damage resistance protein 1, human and bovine serum albumin, and intestinal fatty acid binding protein, in addition to other CYP isoforms. Furthermore, disruption of these interactions can lead to altered paths of metabolism and the production of toxic metabolites. In this review, we summarize the available evidence for CYP proteinprotein interactions from the literature and offer a discussion of the potential impact of future studies aimed at characterizing noncanonical proteinprotein interactions with CYP enzymes.
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