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Divinyl ether synthase from garlic ( Allium sativum L.) bulbs: sub‐cellular localization and substrate regio‐ and stereospecificity
Author(s) -
Grechkin Alexander N.,
Hamberg Mats
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00536-4
Subject(s) - allium sativum , stereospecificity , allium , substrate (aquarium) , chemistry , liliaceae , bulb , ether , biochemistry , atp synthase , botany , stereochemistry , enzyme , biology , organic chemistry , catalysis , ecology
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](9 Z ,11 E ,13 S )‐13‐hydroperoxy‐9,11‐octa‐decadienoic 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.