Reprint

Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 2.0

Edited by
June 2021
286 pages
  • ISBN978-3-0365-0256-4 (Hardback)
  • ISBN978-3-0365-0257-1 (PDF)

This book is a reprint of the Special Issue Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 2.0 that was published in

Biology & Life Sciences
Chemistry & Materials Science
Medicine & Pharmacology
Summary

This book, "Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity", presents five papers on human cytochrome P450 (CYP) and P450 reductase, three reviews on the role of CYPs in humans and their use as biomarkers, six papers on CYPs in microorganisms, and one study on CYP in insects.

The first paper reports the in silico modeling of human CYP3A4 access channels. The second uses structural methods to explain the mechanism-based inactivation of CYP3A4 by mibefradil, 6,7-dihydroxy-bergamottin, and azamulin. The third article compares electron transfer in CYP2C9 and CYP2C19 using structural and biochemical methods, and the fourth uses kinetic methods to study electron transfer to CYP2C8 allelic mutants. The fifth article characterizes electron transfer between the reductase and CYP using in silico and in vitro methods, focusing on the conformations of the reductase.

Then, two reviews describe clinical implications in cardiology and oncology and the role of fatty acid metabolism in cardiology and skin diseases. The second review is on the potential use of circulating extracellular vesicles as biomarkers.

Five papers analyze the CYPomes of diverse microorganisms: the Bacillus genus, Mycobacteria, the fungi Tremellomycetes, Cyanobacteria, and Streptomyces. The sixth focuses on a specific Mycobacterium CYP, CYP128, and its importance in M. tuberculosis.

The subject of the last paper is CYP in Sogatella furcifera, a plant pest, and its resistance to the insecticide sulfoxaflor.

Format
  • Hardback
License
© 2022 by the authors; CC BY-NC-ND license
Keywords
Antibiotics; Bacillus; biosynthetic gene clusters; comparative analysis; cytochrome P450 monooxygenase; Mycobacterium; P450 diversity percentage; P450 profiling; secondary metabolites; NADPH-cytochrome P450 reductase (CPR); microsomal cytochrome P450 (CYP); Cytochrome b5 (CYB5); protein dynamics; electron-transfer (ET); protein–protein interaction; cytochromes P450; CYP3A4; active site access channels; cavities boundaries; minimal cost paths; biosynthetic gene clusters; cytochrome P450 monooxygenase; CYP139A1; genome data mining; host metabolism; Mycobacterium tuberculosis; polyketides; secondary metabolites; tuberculosis; cryptococcus; cryptococcus neoformans; cytochrome P450 monooxygenase; CYP51; fungal pathogens; genome data-mining; human pathogens; CYP diversity analysis; tremellomycetes; trichosporon; CYP3A4; mechanism-based inhibitor; crystal structure; CYP4 genes; genetic polymorphisms; 20-HETE; fatty acid; arachidonic acid; SNPs; molecular functionality; metabolism; lamellar ichthyosis; Bietti’s crystalline dystrophy; cytochrome P450; isoform; membrane protein; protein-membrane interactions; enzyme substrate specificity; mutagenesis; molecular dynamics simulation; Sogatella furcifera; sulfoxaflor; transcriptome; cytochrome P450 monooxygenase; RNA interference; CYP2C8; polymorphisms; reactive oxygen species; paclitaxel; cytochrome P450 reductase; electron transfer; extracellular vesicles; exosomes; cytochrome P450; extrahepatic tissues; plasma; circulatory CYPs; CYP450; drug metabolism; precision Cardio-Oncology; precision medicine; systems medicine; cytochromes P450 monooxygenases; secondary metabolites; Cyanobacteria; biosynthetic gene clusters; gene-cluster diversity percentage; mathematical formula; phylogenetic analysis; Streptomyces; Mycobacterium; Bacillus; Cyanobacteria; cytochrome P450 monooxygenases; secondary metabolites; biosynthetic gene clusters; terpenes; polyketides; P450 blooming; non-ribosomal peptides; cytochrome P450 monooxygenenases; CYP128A1; Mycobacterium tuberculosis H37Rv; tuberculosis; molecular dynamic simulations; azole drugs; menaquinone