Cytochrome P450 1A1 opens up to new substrates.
Article Details
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Munro AW
Cytochrome P450 1A1 opens up to new substrates.
J Biol Chem. 2018 Dec 14;293(50):19211-19212. doi: 10.1074/jbc.H118.006715. Epub 2018 Dec 14.
- PubMed ID
- 30552114 [ View in PubMed]
- Abstract
The cytochromes P450 (CYPs) oxidatively transform a huge number of substrates in both prokaryotic and eukaryotic organisms, but the mechanisms by which they accommodate these diverse molecules remain unclear. A new study by Bart and Scott reports two co-crystal structures of CYP1A1 that reveal structural rearrangements and flexible interaction networks that explain how the active site cavity shapes itself around new ligands. These data open the door to an increased understanding of fundamental enzyme behavior and improved searches for anti-cancer compounds.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Difloxacin Cytochrome P450 1A1 Protein Humans UnknownSubstrateDetails