Long-chain saturated fatty acids can be alpha-oxidised by a purified enzyme (M(r) 240,000) in cucumber (Cucumis sativus).
An enzyme (M(r) 240,000) with high fatty acid alpha-oxidation activity has been purified from the fruit of cucumber (Cucumis sativus). The specific alpha-oxidation activity in the purified fraction was 370 nmol/min per mg protein determined as liberation of 14CO2 from [1-14C]palmitic acid. alpha-Oxidation activity was observed both in the 12,000 x g pellet and 150,000 x g pellet by differential fractionation of cucumber homogenate. The enzyme was purified about 220-fold to near homogeneity from a 12,000 x g fraction by solubilisation with Triton X-100R, ammonium sulphate precipitation, hydrophobic interaction and anion-exchange chromatographies and Superose 12 gel filtration. The molecular mass of the native enzyme was 240,000, and the major subunit molecular mass of 40,000 indicated an oligomeric structure.
Borge
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Norwegian Food Research Institute, As, Norway. grethe.iren.andersen@matforsk.nlh.no
Slinde
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Nilsson
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D002245:Carbon Dioxide / Q000378:metabolism; D002458:Cell Fractionation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D018553:Cucumis sativus / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000378:metabolism*; D008401:Gas Chromatography-Mass Spectrometry; D007700:Kinetics; D008970:Molecular Weight; D010084:Oxidation-Reduction; D019308:Palmitic Acid / Q000378:metabolism; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation
D005227:Fatty Acids; D010940:Plant Proteins; D002245:Carbon Dioxide; D019308:Palmitic Acid