8-[(1R,2R)-3-oxo-2-[(Z)-pent-2-enyl]cyclopentyl]octanoate

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 8-[(1R,2R)-3-oxo-2-[(Z)-pent-2-enyl]cyclopentyl]octanoate
• 化学式: C18H29O3-
• 分子量: 293.4
• InChiKey: BZXZFDKIRZBJEP-GTOOTHNYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  5.3
• 重原子数：
  21
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  57.2
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  NADP⁺ 、 8-[(1R,2R)-3-oxo-2-[(Z)-pent-2-enyl]cyclopentyl]octanoate 生成 (15Z)-12-Oxophyto-10,15-dienoate 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  Characterization of 12-Oxo-Phytodienoic Acid Reductase in Corn

  摘要：

  12-氧代-植物二烯酸还原酶是一种生物合成途径中的酶，可将亚麻酸转化为茉莉酸，该酶已在玉米（Zea mays L.）的籽粒和幼苗中鉴定。通过凝胶过滤法估计，该酶的分子量为54,000。在pH值6.8至9.0的较宽范围内，观察到酶的最佳活性。该酶的底物12-氧代-植物二烯酸的Km为190微摩尔。首选还原剂为NADPH，该酶对NADPH的Km为13微摩尔，而对NADH的Km为4.2毫摩尔。玉米籽粒中的还原酶活性较低，但在发芽后的第五天增加五倍，然后逐渐下降。

  DOI：

  10.1104/pp.80.1.202

文献信息

• Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana
  作者：Lucie Kienow、Katja Schneider、Michael Bartsch、Hans-Peter Stuible、Hua Weng、Otto Miersch、Claus Wasternack、Erich Kombrink

  DOI：10.1093/jxb/erm325

  日期：2008.2

  Arabidopsis thaliana contains a large number of genes encoding carboxylic acid-activating enzymes, including long-chain fatty acyl-CoA synthetase (LACS), 4-coumarate:CoA ligases (4CL), and proteins closely related to 4CLs with unknown activities. The function of these 4CL-like proteins was systematically explored by applying an extensive substrate screen, and it was uncovered that activation of fatty acids is the common feature of all active members of this protein family, thereby defining a new group of fatty acyl-CoA synthetase, which is distinct from the known LACS family. Significantly, four family members also displayed activity towards different biosynthetic precursors of jasmonic acid (JA), including 12-oxo-phytodienoic acid (OPDA), dinor-OPDA, 3-oxo-2(2′-[Z]-pentenyl)cyclopentane-1-octanoic acid (OPC-8), and OPC-6. Detailed analysis of in vitro properties uncovered significant differences in substrate specificity for individual enzymes, but only one protein (At1g20510) showed OPC-8:CoA ligase activity. Its in vivo function was analysed by transcript and jasmonate profiling of Arabidopsis insertion mutants for the gene. OPC-8:CoA ligase expression was activated in response to wounding or infection in the wild type but was undetectable in the mutants, which also exhibited OPC-8 accumulation and reduced levels of JA. In addition, the developmental, tissue- and cell-type specific expression pattern of the gene, and regulatory properties of its promoter were monitored by analysing promoter::GUS reporter lines. Collectively, the results demonstrate that OPC-8:CoA ligase catalyses an essential step in JA biosynthesis by initiating the β-oxidative chain shortening of the carboxylic acid side chain of its precursors, and, in accordance with this function, the protein is localized in peroxisomes.

  拟南芥含有大量编码羧酸活化酶的基因，包括长链脂肪酰基-CoA 合成酶（LACS）、4-香豆酸：CoA 连接酶（4CL）以及与 4CL 密切相关但活性未知的蛋白。通过广泛的底物筛选，系统地探索了这些 4CL 类蛋白质的功能，发现脂肪酸的活化是该蛋白家族所有活性成员的共同特征，从而定义了一组新的脂肪酰基-CoA 合成酶，与已知的 LACS 家族不同。值得注意的是，四个家族成员还对茉莉酸（JA）的不同生物合成前体表现出活性，包括 12-氧代-2-(2′-[Z]-戊烯基)环戊烷-1-辛酸（OPC-8）和 OPC-6。对体外特性的详细分析发现，各酶的底物特异性存在显著差异，但只有一种蛋白质（At1g20510）显示出 OPC-8:CoA 连接酶活性。通过对拟南芥基因插入突变体进行转录本和茉莉酸酯分析，分析了其体内功能。在野生型中，OPC-8:CoA 连接酶的表达在受伤或感染时被激活，但在突变体中却检测不到，突变体也表现出 OPC-8 的积累和 JA 水平的降低。此外，还通过分析启动子：：GUS 报告基因系监测了该基因的发育、组织和细胞类型特异性表达模式及其启动子的调控特性。总之，研究结果表明，OPC-8:CoA 连接酶通过启动其前体羧酸侧链的 β-氧化链缩短作用，催化了 JA 生物合成过程中的一个重要步骤。
• 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
  作者：Florian Schaller、Christian Biesgen、Carsten Müssig、Thomas Altmann、Elmar W. Weiler

  DOI：10.1007/s004250050706

  日期：2000.5.16

  In addition to OPR1 and OPR2, two isoenzymes of 12-oxophytodienoate reductase, a third isoform (OPR3) has recently been identified in Arabidopsis thaliana (L.) Heynh. The expression of the OPR3 gene is induced not only by a variety of stimuli, such as touch. wind, wounding, UV-light and application of detergent, but also by brassinosteroids. The three enzymes were expressed in a functional form in Escherichia coli, and OPR2 was additionally expressed in insect cell cultures and overexpressed in A. thaliana. Substrate conversion was analyzed using a stereospecific assay. The results show that OPR3 effectively converts the natural (9S,13S)-12-oxophytodienoic acid [K-m = 35 mu M, V-max 53.7 nkat (mg protein)(-1)] to the corresponding 3-2(2'(Z)-pentenyl) cyclopentane-1-octanoic acid (OPC-8:0) stereoisomer while OPR1 and OPR2 convert (9S,13S)-12-oxophytodienoic acid with greatly reduced efficiency compared to OPR3. Thus, OPR3 is the isoenzyme relevant for jasmonate biosynthesis.
• ——
  作者：Cínthia Losano Costa、Paulo Arruda、Celso Eduardo Benedetti

  DOI：10.1023/a:1006464822434

  日期：——

  The regulation of genes in response to wounding is mediated in part by the octadecanoids 12-oxo-phytodienoic acid (OPDA), jasmonic acid (JA) and its methyl ester methyl jasmonate (MeJA). We identified, by differential display, an Arabidopsis gene (OPR3) induced after wounding. OPR3 is homologous to members of the flavin mononucleotide (FMN) binding proteins, including the old yellow enzyme (OYE) from yeast and 12-oxophytodienoate-10,11-reductase (OPR) from Arabidopsis. Transcripts of OPR3 rapidly accumulated in leaves after wounding and MeJA treatment, but they were detected in various tissues of unwounded plants at relatively low levels. Expression of the OPR3 gene was significantly reduced in wounded leaves of the coi1 mutant, indicating partial dependence on jasmonate perception for full induction of the gene. The recombinant protein of OPR3 cross-reacted with an antiserum raised against the OYE protein, and showed oxidation of beta -NADPH when OPDA or 15-deoxy-Delta (12,14)-prostaglandin J2 (PGJ2), an analogue of OPDA, was used as substrate. beta -NADPH oxidation was not observed when MeJA, which lacks the double bond in the ketone ring, was used as substrate. The recombinant OPR3 protein also showed beta -NADPH oxidation activity in the presence of cyclohexenone, but not cyclohexanone, suggesting that the enzyme has specificity to cleavage of olefinic bonds in cyclic enones. The results show that the OPR3 gene product represents a new OPR of Arabidopsis induced after wounding.
• Identification of the OsOPR7 gene encoding 12-oxophytodienoate reductase involved in the biosynthesis of jasmonic acid in rice
  作者：Tomoyuki Tani、Hiroyuki Sobajima、Kazunori Okada、Tetsuya Chujo、Shin-ichi Arimura、Nobuhiro Tsutsumi、Mikio Nishimura、Hideharu Seto、Hideaki Nojiri、Hisakazu Yamane

  DOI：10.1007/s00425-007-0635-7

  日期：2008.2

  Enzyme 12-oxophytodienoate (OPDA) reductase (EC1.3.1.42), which is involved in the biosynthesis of jasmonic acid (JA), catalyses the reduction of 10, 11-double bonds of OPDA to yield 3-oxo-2-(2'-pentenyl)-cyclopentane-1-octanoic acid (OPC-8:0). The rice OsOPR1 gene encodes OPDA reductase (OPR) converting (-)-cis-OPDA preferentially, rather than (+)-cis-OPDA, a natural precursor of JA. Here, we provide evidence that an OPR family gene in rice chromosome 8, designated OsOPR7, encodes the enzyme involved in the JA biosynthesis. Recombinant OsOPR7-His protein efficiently catalysed the reduction of both enantiomers of cis-OPDA, similar to the OPR3 protein in Arabidopsis thaliana (L.) Heynh. The expression of OsOPR7 mRNA was induced and reached maximum levels within 0.5 h of mechanical wounding and drought stress, and the endogenous JA level started to increase in accordance with the increase in OsOPR7 expression. The GFP-OsOPR7 fusion protein was detected exclusively in peroxisomes in onion epidermal cells. Furthermore, complementation analysis using an Arabidopsis opr3 mutant indicated that the OsOPR7 gene, but not OsOPR1, was able to complement the phenotypes of male sterility in the mutant caused by JA deficiency, and that JA production in the opr3 mutant was also restored by the expression of the OsOPR7 gene. We conclude that the OsOPR7 gene encodes the enzyme catalysing the reduction of natural (+)-cis-OPDA for the JA biosynthesis in rice.
• A Homolog of Old Yellow Enzyme in Tomato
  作者：Jochen Straßner、Andreas Fürholz、Peter Macheroux、Nikolaus Amrhein、Andreas Schaller

  DOI：10.1074/jbc.274.49.35067

  日期：1999.12

  A cDNA was isolated and characterized from a tomato shoot cDNA library, the deduced amino acid sequence of which exhibited similarity with yeast Old Fellow Enzymes (OYEs) and related enzymes of bacterial and plant origin. Sequence identity was particularly high with 12-oxophytodienoate 10,11-reductase (OPR) from Arabidopsis thaliana. The cDNA-encoded protein was expressed as a glutathione S-transferase fusion protein in Escherichia coli and was purified from bacterial extracts. The protein was found to be a flavoprotein catalyzing the NADPH-dependent reduction of the olefinic bond of alpha,beta-unsaturated carbonyl compounds, including 12-oxophytodienoic acid. Thus, the tomato enzyme was termed LeOPR. The catalytic efficiency of LeOPR was highest with N-ethylmaleimide followed by 12-oxophytodienoic acid and maleic acid as substrates. Photoreduction of the LeOPR-bound FMN resulted in the formation of a red, anionic semiquinone prior to the formation of the fully reduced flavin dihydroquinone, Spectroscopic characterization of LeOPR revealed the formation of charge transfer complexes upon titration with para-substituted phenolic compounds, a distinctive feature of the enzymes of the OYE family. The ligand binding properties were compared between LeOPR and OYE, and the findings are discussed with respect to structural differences between the active sites of OYE and LeOPR.