Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768119 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
The lipoxygenase gene family can synthesize an array of chiral hydroperoxy derivatives from polyunsaturated fatty acids. An individual enzyme, however, reacts molecular oxygen on a single position on the carbon chain and in a single stereo configuration. Regiospecificity is regulated by the orientation and depth of substrate entry into the active site. Stereospecificity is a different issue and only recently has experimental support emerged to explain the conceptual basis of stereo control. A key determinant is a single active site residue conserved as an Ala in S lipoxygenases and a Gly in R lipoxygenases; this residue controls R or S stereochemistry by switching the position of oxygenation on the reacting pentadiene of the substrate. In this review, we meld together the factors that control product regio- and stereochemistry into a general model that can account for the specificity of individual lipoxygenase reactions.
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Authors
Gianguido Coffa, Claus Schneider, Alan R. Brash,