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1.
FIGURE 2.

FIGURE 2. From: Desaturases: Emerging Models for Understanding Functional Diversification of Diiron-containing Enzymes.

Schematic representation of the proposed binding modes of substrate (inner) and their respective products (outer). Note the substrate enters the channel from the right-hand side in the extended conformation.

John Shanklin, et al. J Biol Chem. 2009 July 10;284(28):18559-18563.
2.
FIGURE 1.

FIGURE 1. From: Desaturases: Emerging Models for Understanding Functional Diversification of Diiron-containing Enzymes.

Superimposition of the reduced active site of the castor desaturase and the oxidized active site of the ivy desaturase. A, the reduced active site is shown in blue gray, with brown irons and gray water (Wat). The oxidized active site is shown in cyan, with orange iron ions, and the μ-oxo bridge and water are depicted in yellow. B, the active-site residues of the azide complex of the castor desaturase are shown, with colors the same as those described for A and with Thr199 included. The Asp199 side chain of the T199D mutant is superimposed on the structure and is depicted in green. Note that the view is from the opposite face of the active site with respect to A to clearly show the position of the mutation.

John Shanklin, et al. J Biol Chem. 2009 July 10;284(28):18559-18563.

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