Two moles of O2 consumption and one mole of H2O2 formation during cholesterol peroxidation with cholesterol oxidase from Pseudomonas sp. strain ST-200.
Cholesterol oxidase from Pseudomonas sp. strain ST-200 oxidized cholesterol and cholestanol to 6beta-hydroperoxycholest-4-en-3-one and 5alpha-cholestan-3-one respectively. The former was converted spontaneously to several oxysteroids such as 6-hydroxycholest-4-en-3-one and cholest-4-ene-3,6-dione, with the consumption of 2 mol of O(2) and the formation of 1 mol of H(2)O(2) for each mole of cholesterol oxidized. An oxidized form of the cholesterol oxidase dehydrogenates cholesterol, probably to the 5-en-3-one derivative. A reduced form of the enzyme, yielded from the cholesterol dehydrogenation reaction, dioxygenated cholest-5-en-3-one to 6beta-hydroperoxycholest-4-en-3-one.
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama, 226-8051, Japan.
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Doukyu
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Aono
D002784:Cholesterol / Q000737:chemistry*; D002789:Cholesterol Oxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D015227:Lipid Peroxidation; D009682:Magnetic Resonance Spectroscopy; D010100:Oxygen / Q000737:chemistry*; D011549:Pseudomonas / Q000201:enzymology*
D002784:Cholesterol; D006861:Hydrogen Peroxide; D002789:Cholesterol Oxidase; D010100:Oxygen