Lipoxygenase from baker's yeast: purification and properties.
Lipoxygenase activity was extracted from the mitochondrial fraction of baker's yeast and was purified by affinity chromatography on a linoleyl aminoethyl sepharose column. Two lipoxygenases were eluted from the affinity column. The second enzyme eluted was characterized as a true lipoxygenase. The lipoxygenase eluted showed maximum activity at pH 6.5 with a Km of 2.68 X 10(-4) M on linoleate. The reaction products of the second lipoxygenase with linoleate were characterized by u.v., i.r., NMR spectra and mass spectrometry and were found to be: 9-hydroperoxy-octadeca-trans-10,cis-12-dienoic acid and 13-hydroperoxy-octadeca-cis-9,trans-11-dienoic acid.
D006863:Hydrogen-Ion Concentration; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000378:metabolism; D008054:Lipid Peroxides / Q000378:metabolism; D008084:Lipoxygenase / Q000302:isolation & purification / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013057:Spectrum Analysis; D013379:Substrate Specificity
D008041:Linoleic Acids; D008054:Lipid Peroxides; C008285:linoleic acid hydroperoxide; D019787:Linoleic Acid; D008084:Lipoxygenase