Literature DB >> 34272697

Enzyme Kinetics of Oxidative Metabolism-Cytochromes P450.

Ken Korzekwa1.   

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.
© 2021. Springer Science+Business Media, LLC, part of Springer Nature.

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


  28 in total

1.  Structural basis for ligand promiscuity in cytochrome P450 3A4.

Authors:  Marika Ekroos; Tove Sjögren
Journal:  Proc Natl Acad Sci U S A       Date:  2006-09-05       Impact factor: 11.205

2.  Cytochrome P450: the active oxidant and its spectrum.

Authors:  Jonathan Rittle; Jarod M Younker; Michael T Green
Journal:  Inorg Chem       Date:  2010-04-19       Impact factor: 5.165

3.  Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole: insight into P450 conformational plasticity and membrane interaction.

Authors:  Yonghong Zhao; Mark A White; B K Muralidhara; Ling Sun; James R Halpert; C David Stout
Journal:  J Biol Chem       Date:  2005-12-21       Impact factor: 5.157

4.  Nicotine and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes.

Authors:  Natasha M DeVore; Emily E Scott
Journal:  J Biol Chem       Date:  2012-06-14       Impact factor: 5.157

Review 5.  Spectroscopic features of cytochrome P450 reaction intermediates.

Authors:  Abhinav Luthra; Ilia G Denisov; Stephen G Sligar
Journal:  Arch Biochem Biophys       Date:  2010-12-16       Impact factor: 4.013

6.  Comparative study of the affinity and metabolism of type I and type II binding quinoline carboxamide analogues by cytochrome P450 3A4.

Authors:  Upendra P Dahal; Carolyn Joswig-Jones; Jeffrey P Jones
Journal:  J Med Chem       Date:  2011-12-01       Impact factor: 7.446

7.  Cooperativity in oxidations catalyzed by cytochrome P450 3A4.

Authors:  Y F Ueng; T Kuwabara; Y J Chun; F P Guengerich
Journal:  Biochemistry       Date:  1997-01-14       Impact factor: 3.162

Review 8.  Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation.

Authors:  Ulrich M Zanger; Matthias Schwab
Journal:  Pharmacol Ther       Date:  2013-01-16       Impact factor: 12.310

9.  Multiple substrate binding by cytochrome P450 3A4: estimation of the number of bound substrate molecules.

Authors:  Yury Kapelyukh; Mark J I Paine; Jean-Didier Maréchal; Michael J Sutcliffe; C Roland Wolf; Gordon C K Roberts
Journal:  Drug Metab Dispos       Date:  2008-07-21       Impact factor: 3.922

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  1 in total

1.  Midazolam as a Probe for Heterotropic Drug-Drug Interactions Mediated by CYP3A4.

Authors:  Ilia G Denisov; Yelena V Grinkova; Mark A McLean; Tyler Camp; Stephen G Sligar
Journal:  Biomolecules       Date:  2022-06-20
  1 in total

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