| Literature DB >> 34272697 |
Abstract
The cytochrome P450 enzymes (CYPs) are the most important enzymes in the oxidative metabolism of hydrophobic drugs and other foreign compounds (xenobiotics). The versatility of these enzymes results in some unusual kinetic properties, stemming from the simultaneous interaction of multiple substrates with the CYP active site. Often, the CYPs display kinetics that deviate from standard hyperbolic saturation or inhibition kinetics. Non-Michaelis-Menten or "atypical" saturation kinetics include sigmoidal, biphasic, and substrate inhibition kinetics (see Chapter 2 ). Interactions between substrates include competitive inhibition, noncompetitive inhibition, mixed inhibition, partial inhibition, activation, and activation followed by inhibition (see Chapters 4 and 6 ). Models and equations that can result in these kinetic profiles will be presented and discussed.Entities:
Keywords: Biphasic kinetics; Catalytic cycle; Cytochrome P450; Non-Michaelis-Menten kinetics; Substrate binding
Year: 2021 PMID: 34272697 DOI: 10.1007/978-1-0716-1554-6_9
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745