Abstract
Polyunsaturated fatty acid metabolism is governed primarily by two enzymes, prostaglandin H synthase and lipoxygenase. The crystal structure of the metastable product-oxidized purple form of soybean lipoxygenase-3 was determined at 2.0 A resolution. The data reveal that the chromophore corresponds to an iron-peroxide complex, a potential intermediate in the catalyzed reaction. A significant alteration of the iron site accompanies the formation of the complex. The structure, the first for a fatty acid-lipoxygenase complex, also reveals an unexpected mode of binding, and identifies amino acid residues that may play significant roles in catalysis, regio- and stereoselectivity.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Catalysis
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Crystallography, X-Ray
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Electron Spin Resonance Spectroscopy
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Ferric Compounds / chemistry
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Ferric Compounds / metabolism
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Glycine max / enzymology
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Linoleic Acids / chemistry
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Linoleic Acids / metabolism
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Lipid Peroxides / chemistry
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Lipid Peroxides / metabolism
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Lipoxygenase / chemistry*
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Lipoxygenase / metabolism
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Models, Molecular
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Peroxides / chemistry
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Peroxides / metabolism
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Plant Proteins / chemistry*
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Plant Proteins / metabolism
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Protein Conformation
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Spectrophotometry, Ultraviolet
Substances
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Ferric Compounds
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Linoleic Acids
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Lipid Peroxides
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Peroxides
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Plant Proteins
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13-hydroperoxy-9,11-octadecadienoic acid
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lipoxygenase 3
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Lipoxygenase