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Lipoxygenase from baker's yeast: purification and properties
The International Journal of Biochemistry
|January 1, 1983
Summary
Researchers purified a lipoxygenase enzyme from baker's yeast mitochondria. This enzyme converts linoleate into specific hydroperoxy fatty acids, offering insights into yeast metabolism.
Area of Science:
- Biochemistry
- Enzymology
- Yeast Biology
Background:
- Lipoxygenases are enzymes involved in fatty acid metabolism.
- Mitochondrial lipoxygenase activity in baker's yeast (Saccharomyces cerevisiae) has not been extensively characterized.
Purpose of the Study:
- To isolate and characterize lipoxygenase activity from the mitochondrial fraction of baker's yeast.
- To identify the reaction products of the purified yeast lipoxygenase.
Main Methods:
- Extraction of lipoxygenase activity from yeast mitochondria.
- Purification using affinity chromatography on linoleyl aminoethyl sepharose.
- Characterization of enzyme kinetics (pH optimum, Km) and reaction products using spectroscopic and spectrometric techniques (UV, IR, NMR, Mass Spectrometry).
Main Results:
- Two lipoxygenase activities were separated by affinity chromatography.
- The second purified lipoxygenase exhibited optimal activity at pH 6.5 with a Km of 2.68 x 10(-4) M for linoleate.
- The reaction products were identified as 9-hydroperoxy-octadeca-trans-10,cis-12-dienoic acid and 13-hydroperoxy-octadeca-cis-9,trans-11-dienoic acid.
Conclusions:
- A true lipoxygenase was purified from baker's yeast mitochondria.
- The enzyme catalyzes the formation of specific hydroperoxy fatty acids from linoleate.
- This study provides biochemical characterization of a novel yeast lipoxygenase and its metabolic products.