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1 Naphthyl Acetate

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Masahito Hayatsu – One of the best experts on this subject based on the ideXlab platform.

  • Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100.
    Applied and environmental microbiology, 2002
    Co-Authors: Masayuki Hashimoto, Mitsuru Fukui, Kouichi Hayano, Masahito Hayatsu

    Abstract:

    Rhizobium sp. strain AC100, which is capable of degrading carbaryl (1Naphthyl-N-methylcarbamate), was isolated from soil treated with carbaryl. This bacterium hydrolyzed carbaryl to 1-naphthol and methylamine. Carbaryl hydrolase from the strain was purified to homogeneity, and its N-terminal sequence, molecular mass (82 kDa), and enzymatic properties were determined. The purified enzyme hydrolyzed 1Naphthyl Acetate and 4-nitrophenyl Acetate indicating that the enzyme is an esterase. We then cloned the carbaryl hydrolase gene (cehA) from the plasmid DNA of the strain and determined the nucleotide sequence of the 10-kb region containing cehA. No homologous sequences were found by a database homology search using the nucleotide and deduced amino acid sequences of the cehA gene. Six open reading frames including the cehA gene were found in the 10-kb region, and sequencing analysis shows that the cehA gene is flanked by two copies of insertion sequence-like sequence, suggesting that it makes part of a composite transposon.

  • Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501
    Applied and environmental microbiology, 1993
    Co-Authors: Masahito Hayatsu, Tadahiro Nagata

    Abstract:

    A bacterium capable of hydrolyzing carbaryl (1Naphthyl– N -methylcarbamate) was isolated from a soil enrichment. This bacterium was characterized taxonomically as a Blastobacter sp. and designated strain M501. A carbaryl hydrolase present in this strain was purified to homogeneity by protamine sulfate treatment, ammonium sulfate precipitation, and hydrophobic, anion-exchange, gel filtration, and hydroxylapatite chromatographies. The native enzyme had a molecular mass of 166,000 Da and was composed of two subunits with molecular masses of 84,000 Da. The optimum pH and temperature of the enzyme activity were 9.0 and 45°C, respectively. The enzyme was not stable at temperatures above 40°C. The purified enzyme hydrolyzed seven N -methylcarbamate insecticides and also exhibited activity against 1Naphthyl Acetate and 4-nitrophenyl Acetate. Images

Paul J. Semtner – One of the best experts on this subject based on the ideXlab platform.

  • Diagnostic esterases and insecticide resistance in the tobacco aphid, Myzus nicotianae Blackman (Homoptera: Aphididae)
    Pesticide Biochemistry and Physiology, 1992
    Co-Authors: Yehia A.i. Abdel-aal, E. P. Lampert, R. M. Roe, Paul J. Semtner

    Abstract:

    Abstract Insecticide resistance in the tobacco aphid, Myzus nicotianae Blackman, from different localities in the southeastern United States has been found to exist mainly in aphids with red body coloration. Frequency distribution of esterase activity in individual tobacco aphids collected from a tobacco field and a greenhouse indicated that organophosphate resistance was always linked to high carboxylesterase activity toward 1Naphthyl Acetate. Two approaches were taken to speed up the detection methodology of the frequency of resistant phenotypes. First, an abbreviated bioassay test, using malathion as a reporter molecule, was developed to rapidly distinguish between OP-resistant and susceptible phenotypes of the tobacco aphid. A time threshold of 50 min following aphid exposure to 50 ppm malathion in a water suspension accurately discriminated between susceptible and resistant phenotypes. Second, assays of aphid carboxylesterases, using the Acetates and propionates of 1-naphthol, 2-naphthol, and 4-nitrophenol, were performed to optimize and better understand the esterase discriminating activity between resistant and susceptible phenotypes. Only activity toward 1-naphtholic esters unambiguously discriminated between susceptible and resistant aphids. In general, resistance to malathion appeared to be esterase-mediated and some electrofocusing-detectable esterase isozymes were associated with resistance.

R. M. Roe – One of the best experts on this subject based on the ideXlab platform.

  • Multiple Mechanisms of Pyrethroid Resistance in the German Cockroach, Blattella germanica (L.)
    Pesticide Biochemistry and Physiology, 1994
    Co-Authors: D. D. Anspaugh, Randy L. Rose, P.g. Koehler, Ernest Hodgson, R. M. Roe

    Abstract:

    Abstract Pyrethroid-resistant German cockroaches known as the Village Green strain were compared to a susceptible (Orlando Normal) strain in respect to possible mechanisms of insecticide resistance. Male adults of the resistant strain weighed 15% more than susceptible roaches of the same cumulative age from adult eclosion. Based on the topical application of different concentrations of permethrin, the KD 50 for resistant roaches was 20-times greater than that for susceptible insects. Reduced penetration of [ 14 C]permethrin was observed in resistant insects during 24 hr after treatment along with increased in vivo metabolism as compared with susceptible controls. The cytochrome P450 content and monooxygenase activity when measured with methoxyresorufin and benzo[ a ]pyrene was elevated in resistant roaches by as much as 6.9-fold but no difference was found with benzphetamine. The glutathione transferase activity was also increased (1.6-fold with chlorodinitrobenzene) and elevated esterase activity was detected with the substrates, 1Naphthyl Acetate (1.7-fold) and p -nitrophenyl Acetate (2.1-fold). Using isoelectric focusing, a novel E 2 esterase was identified in resistant cockroaches not found in the susceptible population. E 2 may be partly responsible for the increased esterase activity observed in resistant roaches. Increased esterase activity toward p -nitrophenyl Acetate was used to develop a kinetic, diagnostic assay that could rapidly discriminate resistant from susceptible individuals.

  • Diagnostic esterases and insecticide resistance in the tobacco aphid, Myzus nicotianae Blackman (Homoptera: Aphididae)
    Pesticide Biochemistry and Physiology, 1992
    Co-Authors: Yehia A.i. Abdel-aal, E. P. Lampert, R. M. Roe, Paul J. Semtner

    Abstract:

    Abstract Insecticide resistance in the tobacco aphid, Myzus nicotianae Blackman, from different localities in the southeastern United States has been found to exist mainly in aphids with red body coloration. Frequency distribution of esterase activity in individual tobacco aphids collected from a tobacco field and a greenhouse indicated that organophosphate resistance was always linked to high carboxylesterase activity toward 1Naphthyl Acetate. Two approaches were taken to speed up the detection methodology of the frequency of resistant phenotypes. First, an abbreviated bioassay test, using malathion as a reporter molecule, was developed to rapidly distinguish between OP-resistant and susceptible phenotypes of the tobacco aphid. A time threshold of 50 min following aphid exposure to 50 ppm malathion in a water suspension accurately discriminated between susceptible and resistant phenotypes. Second, assays of aphid carboxylesterases, using the Acetates and propionates of 1-naphthol, 2-naphthol, and 4-nitrophenol, were performed to optimize and better understand the esterase discriminating activity between resistant and susceptible phenotypes. Only activity toward 1-naphtholic esters unambiguously discriminated between susceptible and resistant aphids. In general, resistance to malathion appeared to be esterase-mediated and some electrofocusing-detectable esterase isozymes were associated with resistance.