Purification of lipoxygenase and hydroperoxide dehydrase in flaxseeds: interaction between these enzymatic activities.
We have purified two enzymic activities from flaxseed acetone powder: a lipoxygenase and a hydroperoxide dehydrase. The lipoxygenase activity belongs to an iron-containing protein having a molecular weight of 130 kDa which, upon incubation with alpha-linolenic acid, forms 13-hydroperoxy-9(Z), 11(E), 15(Z)- octadecatrienoic acid. The hydroperoxide dehydrase (a 55 kDa protein) metabolizes this hydroperoxide to an allene oxide which in turn is spontaneously hydrolyzed to alpha- and gamma-ketols. Relationships between these two enzymes were studied and results suggest an inhibition of the lipoxygenase by hydroperoxide dehydrase.
Rabinovitch-Chable
H
H
U.R.A. C.N.R.S. 1485, Faculté de Médecine, Limoges, France.
Cook-Moreau
J
J
Breton
J C
JC
Rigaud
M
M
D002850:Chromatography, Gel; D006836:Hydro-Lyases / Q000302:isolation & purification* / Q000378:metabolism*; D007700:Kinetics; D008042:Linolenic Acids / Q000378:metabolism; D008084:Lipoxygenase / Q000302:isolation & purification* / Q000378:metabolism*; D012639:Seeds / Q000201:enzymology*; D017962:alpha-Linolenic Acid
D008042:Linolenic Acids; D017962:alpha-Linolenic Acid; D008084:Lipoxygenase; D006836:Hydro-Lyases; C057374:hydroperoxide dehydratase