Structural characterization of hydroperoxide lyase in dodecyl maltoside by using circular dichroism.
Fatty acid hydroperoxide lyase (HPL) is a membrane protein, member of the lipoxygenase pathway, which holds a central role in plant defense. Green bell pepper fatty acid hydroperoxide lyase, overexpressed in Escherichia coli, was purified and solubilized in two different non ionic detergents, Triton X-100 and dodecyl maltoside (DM). DM is considered to be more useful compared to Triton X-100, as it allows characterization of the protein with spectroscopic techniques, for which Triton X-100 was inapplicable. Circular dichroism demonstrated that HPL's secondary structure in DM consists of 13.53 % α-helix, 32.73 % β-sheet, 21.76 % turn and 31.13 % unordered.
Department of Chemistry, University of Crete, P.O. Box 2208, 71003, Voutes-Heraklion, Greece.
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Panagakou
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Touloupakis
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Ghanotakis
D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D000595:Amino Acid Sequence; D002212:Capsicum / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D002942:Circular Dichroism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D005960:Glucosides; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017433:Protein Structure, Secondary
D005960:Glucosides; D010940:Plant Proteins; C040358:dodecyl maltoside; D003577:Cytochrome P-450 Enzyme System; D000446:Aldehyde-Lyases; C054540:hydroperoxide lyase