{"title":"Recovery of Ethylene Forming Enzyme from Green Pea Pods","authors":"C. Njoroge, E. Kerbel","doi":"10.1080/00128325.2004.11663412","DOIUrl":null,"url":null,"abstract":"Ethylene Forming Enzyme (EFE) is the enzyme that catalyses the final step in the biosynthesis of ethylene (Kende, 1990; Yang etal., 1990; Yang and Hoffinan, 1984). The site of location of this enzyme in the plant cell is still unknown with certainty.' Mattoo and Lieberman (1977) suggested that it is localised in a cell wall-cell membrane complex. Bouzayen et al., 1990) suggested that there are two sites for EFE location in a plant cell. One of the sites is located on the plasmalemma and is very sensitive to plasmolysis of the cell, and the other site is in the tonoplast and its ethylene-forming ability is not affected by plasmolysis. These authors excluded the cell wall as a possible site for EFE location. Ververidis and John (1990) confirmed the findings of Bouzayens etal.; and also suggested that the actual EFE location depends on the stage of plant growth. Irrespective of the site of EFE location, it had been felt that it could only oxidise 1aminocyclopropane-carboxylic acid (ACC) to ethylene effectively if bound to the membrane, as its activity had not been recovered in vitro (John et al., 1985; Venis, 1984; Porter et al., 1986; Mayne and Kende, 1986). However, Ververidis and John (1991), fully recovered EFE activity in a cell free system from melon (Cucurnis melo) fruits. Other cell free systems have been reported to oxidise ACC to ethylene, but all the systems have a very high K,„ for ACC in the plant and this rules out the possibility of such systems being operative in the plant systems in-vivo because of their high Kin values for ACC. (McKeon and Yang, 1984; Stegink et al., 1986; Nielsen et al., 1984; Venis, 1984; Mayak etal., 1981).","PeriodicalId":11421,"journal":{"name":"East African Agricultural and Forestry Journal","volume":"5 1","pages":"1 - 6"},"PeriodicalIF":0.0000,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"East African Agricultural and Forestry Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/00128325.2004.11663412","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Ethylene Forming Enzyme (EFE) is the enzyme that catalyses the final step in the biosynthesis of ethylene (Kende, 1990; Yang etal., 1990; Yang and Hoffinan, 1984). The site of location of this enzyme in the plant cell is still unknown with certainty.' Mattoo and Lieberman (1977) suggested that it is localised in a cell wall-cell membrane complex. Bouzayen et al., 1990) suggested that there are two sites for EFE location in a plant cell. One of the sites is located on the plasmalemma and is very sensitive to plasmolysis of the cell, and the other site is in the tonoplast and its ethylene-forming ability is not affected by plasmolysis. These authors excluded the cell wall as a possible site for EFE location. Ververidis and John (1990) confirmed the findings of Bouzayens etal.; and also suggested that the actual EFE location depends on the stage of plant growth. Irrespective of the site of EFE location, it had been felt that it could only oxidise 1aminocyclopropane-carboxylic acid (ACC) to ethylene effectively if bound to the membrane, as its activity had not been recovered in vitro (John et al., 1985; Venis, 1984; Porter et al., 1986; Mayne and Kende, 1986). However, Ververidis and John (1991), fully recovered EFE activity in a cell free system from melon (Cucurnis melo) fruits. Other cell free systems have been reported to oxidise ACC to ethylene, but all the systems have a very high K,„ for ACC in the plant and this rules out the possibility of such systems being operative in the plant systems in-vivo because of their high Kin values for ACC. (McKeon and Yang, 1984; Stegink et al., 1986; Nielsen et al., 1984; Venis, 1984; Mayak etal., 1981).
乙烯形成酶(EFE)是催化乙烯生物合成最后一步的酶(Kende, 1990;杨等等。, 1990;Yang and Hoffinan, 1984)。这种酶在植物细胞中的位置仍然是未知的。”Mattoo和Lieberman(1977)认为它定位于细胞壁-细胞膜复合体。Bouzayen et al., 1990)认为EFE在植物细胞中有两个位置。其中一个位点位于细胞质膜上,对细胞的质解非常敏感,另一个位点位于细胞质内,其乙烯生成能力不受质解的影响。这些作者排除了细胞壁作为EFE定位的可能位点。Ververidis和John(1990)证实了Bouzayens等人的发现;结果表明,EFE的实际位置取决于植物的生长阶段。无论EFE的位置如何,人们认为它只能在与膜结合时有效地将1氨基环丙烷-羧酸(ACC)氧化为乙烯,因为它的活性在体外没有恢复(John等人,1985;像,1984;Porter et al., 1986;Mayne and Kende, 1986)。然而,Ververidis和John(1991)在甜瓜果实的无细胞系统中完全恢复了EFE活性。据报道,其他无细胞系统将ACC氧化为乙烯,但所有系统都有非常高的K,“对于植物中的ACC,这排除了这些系统在植物体内系统中运作的可能性,因为它们的ACC的Kin值很高。(McKeon and Yang, 1984;Stegink et al., 1986;Nielsen et al., 1984;像,1984;克等等。, 1981)。