Interaction of CYP3A4 with caffeine: First insights into multiple substrate binding

IF Sevrioukova - Journal of Biological Chemistry, 2023 - ASBMB
Human cytochrome P450 3A4 (CYP3A4) is a major drug-metabolizing enzyme that shows
extreme substrate promiscuity. Moreover, its large and malleable active site can …

Structural basis for ligand promiscuity in cytochrome P450 3A4

M Ekroos, T Sjögren - … of the National Academy of Sciences, 2006 - National Acad Sciences
Cytochrome P450 (CYP) 3A4 is the most promiscuous of the human CYP enzymes and
contributes to the metabolism of≈ 50% of marketed drugs. It is also the isoform most often …

Crystal structure of CYP3A4 complexed with fluorol identifies the substrate access channel as a high-affinity ligand binding site

IF Sevrioukova - International Journal of Molecular Sciences, 2022 - mdpi.com
Cytochrome P450 3A4 (CYP3A4) is a major human drug-metabolizing enzyme, notoriously
known for its extreme substrate promiscuity, allosteric behavior, and implications in drug …

[HTML][HTML] Structural perspectives of the CYP3A family and their small molecule modulators in drug metabolism

WC Wright, J Chenge, T Chen - Liver research, 2019 - Elsevier
Cytochrome P450 (CYP) enzymes function to catalyze a wide range of reactions, many of
which are critically important for drug response. Members of the human cytochrome P450 3A …

Insights into the structure, function, and regulation of human cytochrome P450 1A2

SF Zhou, LP Yang, MQ Wei, W Duan… - Current drug …, 2009 - ingentaconnect.com
CYP1A2 is one of the major CYPs in human liver (∼ 13%) and metabolises a variety of
clinically important drugs, such as clozapine, lidocaine, theophylline, tacrine, and …

Unraveling the structural basis of selective inhibition of human cytochrome P450 3A5

J Wang, CD Buchman, J Seetharaman… - Journal of the …, 2021 - ACS Publications
The human cytochrome P450 (CYP) CYP3A4 and CYP3A5 enzymes metabolize more than
one-half of marketed drugs. They share high structural and substrate similarity and are often …

Structural basis for the diminished ligand binding and catalytic ability of human fetal-specific CYP3A7

IF Sevrioukova - International journal of molecular sciences, 2021 - mdpi.com
Cytochrome P450 3A7 (CYP3A7) is a fetal/neonatal liver enzyme that participates in estriol
synthesis, clearance of all-trans retinoic acid, and xenobiotic metabolism. Compared to the …

Structures of cytochrome P450 3A4

EE Scott, JR Halpert - Trends in biochemical sciences, 2005 - cell.com
Cytochrome P450 3A4 (CYP3A4) catalyzes the initial step in the clearance of many
pharmaceuticals and foreign chemicals. The structurally diverse nature of CYP3A4 …

Structure, function, regulation and polymorphism of human cytochrome P450 2A6

YM Di, VDW Chow, LP Yang… - Current drug metabolism, 2009 - ingentaconnect.com
The CYP2A6 gene spans a region of approximately 6 kb pairs consisting of 9 exons and has
been mapped to the long arm of chromosome 19 (between 19q12 and 19q13. 2). The …

Identification of Val117 and Arg372 as critical amino acid residues for the activity difference between human CYP2A6 and CYP2A13 in coumarin 7-hydroxylation

XY He, J Shen, WY Hu, X Ding, AYH Lu… - Archives of Biochemistry …, 2004 - Elsevier
Human cytochrome P450 (CYP) 2A6 and 2A13 play an important role in catalyzing the
metabolism of many environmental chemicals including coumarin, nicotine, and several …