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A P450 Close-up

Enzymes in the cytochrome P450 superfamily play a significant role in the detoxication of foreign compounds and the biosynthesis of several endogenous compounds, including steroid hormones, bile acids, and cholesterol. P450 1A2 is the principal cytochrome family 1 enzyme. It is expressed in the human liver and participates extensively in the hepatic oxidation of a wide range of drugs.

Two views of the structure of P450 1A2.

In this Paper of the Week, Stefaan Sansen and colleagues present the crystal structure of human P450 1A2 in complex with the inhibitor -naphthoflavone at a resolution of 1.95 Å. Their structure reveals a compact, closed active site cavity that is highly adapted for the positioning and oxidation of relatively large, planar substrates. The topology is distinct from the known active site structures of P450 enzymes from other families and demonstrates how P450 family 1 enzymes have evolved to efficiently catalyze the oxidation of polycyclic aromatic hydrocarbons.

FOOTNOTES

See referenced article, J. Biol. Chem. 2007, 282, 14348-14355

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