By Swati Nagar
This publication is split into five components. half I presents the basic ideas of enzyme kinetics. How are those parameters derived? whereas those are basic innovations handled in different texts, what do they honestly suggest from a drug metabolism and shipping standpoint? This e-book goals at answering this question. half II of the e-book makes a speciality of the kinetics of oxidative and conjugative drug metabolizing enzymes and drug transporters. half III considers a few modeling techniques for either drug metabolizing enzymes and transporters. realizing of variability—intrinsic and extrinsic—is handled partly IV and is taken into account an important from “design of experiments” to “interpretation of results.” eventually partly V, case stories supply real-life examples, conversations among manager and scientist, and present outlooks, which offer possibilities from which we will all research.
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Extra resources for Enzyme Kinetics in Drug Metabolism: Fundamentals and Applications
Sample text
The Michaelis–Menten equation represents a rectangular hyperbola, with a y-asymptote at the Vmax value. In many cases, more complex kinetic models are required to explain the observed data. Atypical kinetic profiles are believed to arise from the simultaneous binding of multiple molecules within the active site of the enzyme (Tracy and Hummel, Drug Metab Rev 36:231–242, 2004). Several cytochromes P450 have large active sites that enable binding of multiple molecules (Wester et al. J Biol Chem 279:35630–35637, 2004; Yano et al.
Some examples of artifactual Models of Enzyme Kinetics 33 sources of atypical kinetics include substantial substrate depletion, saturable nonproductive binding of the substrate (or metabolites) within the incubation matrix, poorly defined analytical quantitation limits, and aqueous solubility limitations [10, 22] (see Chapters 7 and 16, and Case Studies 1 and 2). The contribution of multiple enzymes to formation of a single metabolite can also complicate the kinetic profile and may result in the observation of atypical kinetic behaviors (see Chapters 6, 8, and 11, and Case Study 7).
9 and defines the total enzyme concentration as the sum of the free (unbound) enzyme concentration [E]f and the concentration of ES complex: ½E ¼ ½Ef þ ½ES (9) 14 Eleanore Seibert and Timothy S. Tracy Fig. 3 Example of Michaelis–Menten kinetics. In this figure, the Km and Vmax values are 2 and 100, respectively Substituting Eq. 9 into Eq. 8 and dividing through by k1 yields Eq. 10: kÀ1 þ k2 ½ES (10) ½E À ½ES ½S ¼ k1 A new constant, Km, can be defined as in Eq. 11 and substituted into Eq.