10184-66-4Relevant articles and documents
The synthesis and herbicidal evaluation of fluorine-containing phenoxyacetoxyalkylphosphonate derivatives
Chen, Ting,Shen, Ping,Li, Yanjun,He, Hongwu
, p. 2135 - 2145 (2006)
To investigate the influence of a fluorine moiety on the biological activity of phenoxyacetoxyalkylphosphonates, a series of fluorine-containing phenoxyacetoxyalkylphosphonates were synthesized and screened for herbicidal activity in a greenhouse. The majority of the title compounds showed better preemergence activity than postemergence activity against the test plants, especially on monocotyledon. Compound 5l exhibited notable activity. Results showed that by introducing a fluorine moiety to the parent structure of phenoxyacetoxyalkylphosphonates, a series of new compounds with satisfactory herbicidal activity could be synthesized. A reasonable combination of a fluorine moiety and other substituents on the benzene ring had a great influence on the herbicidal activity. Copyright Taylor & Francis Group, LLC.
Enzymes in Organic Chemistry, Part 1: Enantioselective Hydrolysis of α-(Acyloxy)phosphonates by Esterolytic Enzymes
Li, Yong-Fu,Hammerschmidt, Friedrich
, p. 109 - 120 (1993)
α-Hydroxyphosphonates (+/-)-3 were prepared and transformed into esters (+/-)-5.Eight lipases as well as pig liver esterase were tested as catalysts for enantioselective hydrolyses of α-(acyloxy)phosphonates in a biphasic system.Two of them proved to be useful.The highest enantioselectivity was obtained with lipase F-AP 15 and α-(acetyloxy)phenylmethylphosphonates (+/-)-5a and (+/-)-5b as substrates.The (S)-enantiomers were exclusively hydrolyzed to give optically pure alcohols (S)-(-)-3a and (S)-(-)-3b.Lipases AP 6 and F-AP 15 were used to prepare phosphonates(S)-(-)-3b, (S)-(+)-3d and (S)-(-)-3e on a preparative scale with an enantiomeric excess of 81percent, 87percent, and 89percent, respectively.The absolute configurations of the α-hydroxyphosphonates were assigned by Horeau's method and 1H NMR spectroscopy of Mosher's derivatives.
Synthesis and Herbicidal Activity of α-(Substituted Phenoxybutyryloxy or Valeryloxy)alkylphosphonates and 2-(Substituted Phenoxybutyryloxy)alkyl-5,5-dimethyl-1,3,2-dioxaphosphinan-2-one
Wang, Wei,Zhang, Sha-Sha,Zhou, Yuan,Peng, Hao,He, Hong-Wu,Lu, Xing-Tao
, p. 6911 - 6915 (2016/10/03)
On the basis of our work on the modification of alkylphosphonates 1, a series of α-(substituted phenoxybutyryloxy or valeryloxy)alkylphosphonates (4-5) and 2-(substituted phenoxybutyryloxy)alkyl-5,5-dimethyl-1,3,2-dioxaphosphinan-2-one (6) were designed and synthesized. The bioassay results indicated that 14 of title compounds 4 exhibited significant postemergence herbicidal activity against velvetleaf, common amaranth, and false daisy at 150 g ai/ha. Compounds 5 were inactive against all tested weeds. Compounds 6 exhibited moderate to good inhibitory effect against the tested dicotyledonous weeds. Structure-activity relationship (SAR) analyses showed that the length of the carbon chain as linking bridge had a great effect on the herbicidal activity. Broad-spectrum tests of compounds 4-1, 4-2, 4-9, 4-30, and 4-36 were carried out at 75 g ai/ha. Especially, 4-1 exhibited 100% inhibition activity against the tested dicotyledonous weeds, which was higher than that of glyphosate.
Potent inhibition of mandelate racemase by a fluorinated substrate-product analogue with a novel binding mode
Nagar, Mitesh,Lietzan, Adam D.,St. Maurice, Martin,Bearne, Stephen L.
, p. 1169 - 1178 (2014/03/21)
Mandelate racemase (MR) from Pseudomonas putida catalyzes the Mg 2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate. Because trifluorolactate is also a substrate of MR, we anticipated that replacing the phenyl rings of the competitive, substrate-product analogue inhibitor benzilate (Ki = 0.7 mM) with trifluoromethyl groups might furnish an inhibitor. Surprisingly, the substrate-product analogue 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)propanoate (TFHTP) was a potent competitive inhibitor [Ki = 27 ± 4 μM; cf. Km = 1.2 mM for both (R)-mandelate and (R)-trifluorolactate]. To understand the origins of this high binding affinity, we determined the X-ray crystal structure of the MR-TFHTP complex to 1.68 A resolution. Rather than chelating the active site Mg2+ with its glycolate moiety, like other ground state analogues, TFHTP exhibited a novel binding mode with the two trifluoromethyl groups closely packed against the 20s loop and the carboxylate bridging the two active site Bronsted acid-base catalysts Lys 166 and His 297. Recognizing that positioning a carboxylate between the Bronsted acid-base catalysts could yield an inhibitor, we showed that tartronate was a competitive inhibitor of MR (Ki = 1.8 ± 0.1 mM). The X-ray crystal structure of the MR-tartronate complex (1.80 A resolution) revealed that the glycolate moiety of tartronate chelated the Mg2+ and that the carboxylate bridged Lys 166 and His 297. Models of tartronate in monomers A and B of the crystal structure mimicked the binding orientations of (S)-mandelate and that anticipated for (R)-mandelate, respectively. For the latter monomer, the 20s loop appeared to be disordered, as it also did in the X-ray structure of the MR triple mutant (C92S/C264S/K166C) complexed with benzilate, which was determined to 1.89 A resolution. These observations indicate that the 20s loop likely undergoes a significant conformational change upon binding (R)-mandelate. In general, our observations suggest that inhibitors of other enolase superfamily enzymes may be designed to capitalize on the recognition of the active site Bronsted acid-base catalysts as binding determinants.
