109959-41-3Relevant articles and documents
Facile preparation of optically active jasmonates and their biological activities in rice
Miyamoto, Koji,Matsumoto, Tomoharu,Yumoto, Emi,Sakazawa, Tomoko,Yokota, Takao,Yamane, Hisakazu,Uchida, Kenichi
, p. 876 - 881 (2019)
A facile and efficient method has been developed for the optical resolution of racemic jasmonic acid (JA) on a relatively large scale and was successfully utilized for the preparation of optically pure (+)-JA and (?)-JA. We indicated that (+)-JA has lower growth inhibitory activity than (?)-JA in the rice seedling growth test and confirmed in line with an earlier observation that their respective biologically-active forms, (+)-JA-Ile and (?)-JA-Ile, show comparable inhibitory activities. We compared the metabolism of (+)-JA and (?)-JA into (+)-JA-Ile and (?)-JA-Ile, respectively, in the JA-deficient rice cpm2, and found that the exogenously applied (+)-JA was metabolized to the corresponding Ile conjugate less efficiently as compared with (?)-JA. Such metabolic rate difference may cause a discrepancy between biological potencies of (+)-JA and (?)-JA in rice.
Purification and partial amino acid sequences of an esterase from tomato
Stuhlfelder, Christiane,Lottspeich, Friedrich,Mueller, Martin J.
, p. 233 - 240 (2002)
Screening of 18 suspension plant cell cultures of taxonomically distant species revealed that a methyl jasmonate hydrolysing enzyme activity (0.21-5.67 pkat/mg) occurs in all species so far analysed. The methyl jasmonate hydrolysing esterase was purified from cell cultures of Lycopersicon esculentum using a five-step procedure including anion-exchange chromatography, gel-filtration and chromatography on hydroxylapatite. The esterase was purified 767-fold to give an almost homogenous protein in a yield of 2.2%. The native enzyme exhibited a Mr of 26 kDa (gel-filtration chromatography), which was similar to the Mr determined by SDS-PAGE and MALDI-TOF analysis (Mr of 28547 kDa). Enzyme kinetics revealed a Km value of 15 μM and a Vmax value of 7.97 nkat/mg, an pH optimum of 9.0 and a temperature optimum of 40 °C. The enzyme also efficiently hydrolyzed methyl esters of abscisic acid, indole-3-acetic acid, and fatty acids. In contrast, methyl esters of salicylic acid, benzoic acid and cinnamic acid were only poor substrates for the enzyme. N-Methylmaleimide, iodacetamide, bestatin and pepstatin (inhibitors of thiol-, metal- and carboxyproteases, respectively) did not inactivate the enzyme while a serine protease inhibitor, phenylmethylsulfonyl fluoride, at a concentration of 5 mM led to irreversible and complete inhibition of enzyme activity. Proteolysis of the pure enzyme with endoproteinase LysC revealed three peptide fragments with 11-14 amino acids. N-Terminal sequencing yielded an additional peptide fragment with 10 amino acids. Sequence alignment of these fragments showed high homologies to certain plant esterases and hydroxynitrile lyases that belong to the α/β hydrolase fold protein superfamily.
Preparation and biological activity of molecular probes to identify and analyze jasmonic acid-binding proteins
Jikumaru, Yusuke,Asami, Tadao,Seto, Hideharu,Yoshida, Shigeo,Yokoyama, Tadashi,Obara, Naomi,Hasegawa, Morifumi,Kodama, Osamu,Nishiyama, Makoto,Okada, Kazunori,Nojiri, Hideaki,Yamane, Hisakazu
, p. 1461 - 1466 (2007/10/03)
Several types of jasomonic acid (JA) derivatives, including JA-amino acid conjugates, a JA-biotin conjugate, a JA-dexamethasone heterodimer, and a JA-fluoresceine conjugate, were prepared as candidates for molecular probes to identify JA-binding proteins. These JA derivatives, excepting the JA-fluoresceine conjugate, exhibited significant biological activities in a rice seedling assay, a rice phytoalexin-inducing assay, and/or a soybean phenylalanine ammonia-lyase-inducing assay. These JA derivatives could therefore be useful probes for identifying JA-binding proteins. The activity spectra of the prepared compounds were different from each other, suggesting that different types of JA receptors were involved in the perception of JA derivatives in the respective bioassays.
