Mechanistic aspects of CYP74 allene oxide synthases and related cytochrome P450 enzymes.
The existence of CYP5, CYP8A, and the CYP74 enzymes specialized for reaction with fatty acid peroxide substrates presents opportunities for a "different look" at the catalytic cycle of the cytochrome P450s. This review considers how the properties of the peroxide-metabolizing enzymes are distinctive, and how they tie in with those of the conventional monooxygenase enzymes. Some unusual reactions of each class have parallels in the other. As enzyme reactions and P450 structures emerge there will be possibilities for finding their special properties and edging this knowledge into the big picture.
Brash
Alan R
AR
Department of Pharmacology, and the Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, Tennessee 37232, USA. alan.brash@vanderbilt.edu
D000446:Aldehyde-Lyases / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D019746:Intramolecular Oxidoreductases / Q000378:metabolism; D008954:Models, Biological; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000201:enzymology / Q000378:metabolism*; D013930:Thromboxane-A Synthase / Q000378:metabolism
D010940:Plant Proteins; D003577:Cytochrome P-450 Enzyme System; D000446:Aldehyde-Lyases; C054540:hydroperoxide lyase; D019746:Intramolecular Oxidoreductases; C022461:prostacyclin synthetase; D013930:Thromboxane-A Synthase; C021377:hydroperoxide isomerase