title: Divinyl ether synthase from garlic (Allium sativum L.) bulbs: sub-cellular localization and substrate regio-and stereospecificity.
abstract: Sub-cellular localization and some properties of 13-hydroperoxide-specific divinyl ether synthase from garlic bulbs were studied. Sub-cellular fractions from garlic bulbs were incubated with [1-(14)C](9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid (13-HPOD). The predominant part of divinyl ether synthase activity from garlic bulbs was found in the microsomal fraction. The enzyme utilizes 13(S)-HPOD as its preferential substrate. Other hydroperoxides, including 9(S)-HPOD, gave much poorer yields of divinyl ethers. Unreacted hydroperoxide after incubation of 13(R,S)-HPOD with enzyme was composed of up to 94% 13(R)-HPOD. Thus, divinyl ether synthase possesses stereoselectivity, utilizing preferentially the (S)-enantiomer.
authors.affiliation: Institute of Biology, Russian Academy of Sciences, Kazan, Russia.
authors.forename: A N
authors.initials: AN
authors.lastname: Grechkin
authors.forename: M
authors.initials: M
authors.lastname: Hamberg
mesh_terms: D003577:Cytochrome P-450 Enzyme System; D005737:Garlic / Q000201:enzymology*; D008041:Linoleic Acids / Q000378:metabolism; D008054:Lipid Peroxides; D008861:Microsomes / Q000378:metabolism; D008968:Molecular Conformation; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010940:Plant Proteins; D010946:Plants, Medicinal; D013347:Subcellular Fractions; D013379:Substrate Specificity; D014753:Vinyl Compounds / Q000378:metabolism*
chemical_list: D008041:Linoleic Acids; D008054:Lipid Peroxides; D010940:Plant Proteins; D014753:Vinyl Compounds; C038649:13-hydroperoxy-9,11-octadecadienoic acid; C100195:vinyl ether; D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; C100485:divinyl ether synthase