Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8292451 | Biochemical and Biophysical Research Communications | 2018 | 5 Pages |
Abstract
The first crystal structure of a class VII P450, CYP116B46 from Tepidiphilus thermophilus, has been solved at 1.9â¯Ã
resolution. The structure reveals overall conservation of the P450-fold and a water conduit around the I-helix. Active site residues have been identified and sequence comparisons have been made with other class VII enzymes. A structure similarity search demonstrated that the P450-TT structure is similar to enzymes capable of oxy-functionalization of fatty acids, terpenes, macrolides, steroids and statins. The insight gained from solving this structure will provide a guideline for future engineering and modelling studies on this catalytically promiscuous class of enzymes.
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Authors
Michele Tavanti, Joanne L. Porter, Colin W. Levy, J. Rubén Gómez Castellanos, Sabine L. Flitsch, Nicholas J. Turner,