12-氧代植物二烯酸-10,11-还原酶：针对12-氧代植物二烯酸立体异构体具有不同特异性的两种同工酶的存在情况。
12-Oxophytodienoate-10,11-reductase: occurrence of two isoenzymes of different specificity against stereoisomers of 12-oxophytodienoic acid.
作者信息
Schaller F, Hennig P, Weiler EW
机构信息
Lehrstuhl fur Pflanzenphysiologie, Ruhr-Universitat, D-44780 Bochum, Germany.
出版信息
Plant Physiol. 1998 Dec;118(4):1345-51. doi: 10.1104/pp.118.4.1345.
Abstract
The reduction of 12-oxophytodienoic acid (OPDA) to 3-oxo-2(2'[Z]-pentenyl)-cyclopentane-1-octanoic acid is catalyzed by 12-oxophytodienoate-10,11-reductase (OPR). Analysis of the isomer preference of OPR has indicated that the activity is composed of two isoenzymes exhibiting different stereoselectivities. The two isoforms of OPR have been separated, using protein extracts of Rock Harlequin (Corydalis sempervirens) as the starting material. OPRI, the enzyme reported earlier from the same species and corresponding to the cloned OPR from Arabidopsis, utilized 9R,13R-OPDA >> 9S, 13R-OPDA but not the 13S-configured isomers, whereas the new activity, OPRII, effectively reduced all four OPDA isomers, including the natural 9S,13S-OPDA (cis-[+]-OPDA). OPRII activity is characterized in detail. The enzyme's enzymatic, biochemical, and immunological properties prove that it is a close relative of OPRI. The roles of OPRI and OPRII in octadecanoid biology are discussed.
摘要
12-氧代植物二烯酸（OPDA）还原为3-氧代-2(2'[Z]-戊烯基)-环戊烷-1-辛酸是由12-氧代植物二烯酸-10,11-还原酶（OPR）催化的。对OPR异构体偏好性的分析表明，其活性由两种表现出不同立体选择性的同工酶组成。以岩黄连（Corydalis sempervirens）的蛋白质提取物为起始材料，已分离出OPR的两种同工型。OPRI是先前从同一物种中报道的酶，与拟南芥中克隆的OPR相对应，它利用9R,13R-OPDA >> 9S,13R-OPDA，但不利用13S构型的异构体，而新活性OPRII则能有效还原所有四种OPDA异构体，包括天然的9S,13S-OPDA（顺式-[+]-OPDA）。对OPRII的活性进行了详细表征。该酶的酶学、生化和免疫学特性证明它是OPRI的近亲。讨论了OPRI和OPRII在十八烷类生物学中的作用。
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