Resistance to DDT, DDT-Dehydrochlorinase, an Enzyme Found in DDT-Resistant Flies

Sternburg, J. G.; Kearns, C. W.; Moorefield, H. H.

doi:10.1021/jf60042a008

Cited by 81 publications

(21 citation statements)

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“…This mechanism is different from the canonical GST detoxification reaction because no GSH-DDT conjugate is formed. 4 GSH-dependent DDTase activity was first discovered in Musca domestica (housefly), 5 and it was then shown that purified housefly proteins with DDTase activity also had biochemical activities typical of GSTs. 6 Since then, GSTs from Drosophila melanogaster, 7 Anopheles gambiae, 2 Anopheles dirus, 8 and Aedes aegypti 9 have been cloned and shown to have DDTase activity.…”

mentioning

confidence: 99%

Recognition and Detoxification of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1

Low

Feil

et al. 2010

Journal of Molecular Biology

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confidence: 99%

Recognition and Detoxification of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1

Low

Feil

et al. 2010

Journal of Molecular Biology

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“…[1] DDTdehydrohalogenases of the house fly had a pH optimum of 7.4. [26] This enzyme is resistant to digestion by proteolytic enzymes as well as high temperature without undergoing denaturation. [1] The enzyme from Pseudomonas putida T5 at acid and alkaline range showed 95.7 and 95.3% lower activity, respectively.…”

Section: Discussionmentioning

confidence: 99%

PURIFICATION AND CHARACTERIZATION OF DDT-DEHYDROHALOGENASE FROMPseudomonas putidaT5

Latha

Rajagopalan

Singh

et al. 2012

Preparative Biochemistry and Biotechnology

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DDT-dehydrohalogenase is involved in the catalytic degradation of p,p'-DDT by eliminating either HCl or Cl(-) to form DDD/DDE. Isolation, purification and characterization of DDT-dehydrohalogenase from a bacterial source is reported in this manuscript. Ten bacterial cultures belonging to DDT degrading microbial consortium were screened for the DDT-dehydrohalogenase activity. Among these, the clarified cell homogenate of Pseudomonas putida T5 showed higher DDT-dehydrohalogenase activity and enzyme was purified to apparent homogeneity with 73% overall recovery. The relative molecular mass of the enzyme estimated by the SDS PAGE method was ∼32 kDa. Native PAGE revealed the presence of a single band. The purity of the enzyme was confirmed by HPLC and capillary electrophoresis. The enzyme was stable for 4-5 h at pH 7.0 at the temperature optima of 37 °C. The K( m ) and V( max ), values for DDT-dehydrohalogenase were 3.7 µM and 6.8 µM min(-1), respectively. The enzyme was a glycoprotein with mannose forming the backbone. AIG-formed the N-terminus chain. Serine and tryptophan appeared to be involved at the active site. The enzyme appeared to be a metalloprotein containing Zn, Mg, and Ca ions. Monovalent and divalent cations (1 mM) inhibited the enzyme strongly. The primary sequence of HPLC purified enzyme was deduced by LC-MS-MALDI-ESI.

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“…Lichtwardt (1964), Tsukamoto and Suzuki (1964), Oppenoorth (1965a, 1965b and Grigolo and Oppenoorth (1966) found that the dominant gene for DDT resistance (variously named R, D-ase, RDDT) in strains originating in the United States of America and Japan was located in chromosome II. Oppenoorth's work proved that this gene caused the production of the enzyme DDT-dehydrochlorinase, discovered by Sternburg, Kearns, and Moorefield (1954), and indicated the possibility that different alleles of this gene have been selected in strains with various activities of the enzyme. At present it seems likely that the DDT resistance gene of the Canberra colony is allelic with RDDT.…”

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confidence: 99%

Inheritance of Ddt Resistance in a Laboratory Colony of the Housefly, Musca Domestica

Kerr¹

1970

Aust. Jnl. Of Bio. Sci.

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SummaryStrains of the housefly MUBOO domeatica L., derived by selection from the Canberra laboratory colony established in 1939, were examined genetically and cytologically to determine their composition, in respect to resistance to DDT, and the modes of sex determination and inheritance of this resistance.DDT resistance was found to be determined by an incompletely dominant allele of a gene in chromosome II that confers the ability to metabolize DDT to DDE. In flies of the normal karyotype, 2n = 12: XX females and XY males, resistance is inherited independently of sex, but in atypical XX males, lacking the Y -chromosome, the male determinant is linked with presumably the same resistance allele in one of the chromosome II homologues. The resistance gene in this homologue is thus obligatory for, and confined to, atypical males, but on rare occasions is inherited by a female, indicating that the linkage with the male determinant is not completely stable.Atypical males were not detected in the unselected colony. They were brought into prominence by selection either for early adult emergence or for DDT resistance. Under DDT selection pressure, the progression of one strain towards homozygosity for the resistance allele was retarded slightly by the complete replacement of XY males by the atypical XX type, and the strain was still heterogeneous after 200 generations of selection.Each of 10 lines propagated from single homozygous resistant pairs became heterogeneous when mass-reared in the absence of DDT. Instability of the resistance gene may therefore have been a factor opposing selection in the strain under DDT pressure.Rare XXY males and XXX females among flies of the normal karyotype, and rarer XO and XXX males among the XX males of atypical strains, were considered to be products of non-disjunctions. No XO females were found.

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Resistance to DDT, DDT-Dehydrochlorinase, an Enzyme Found in DDT-Resistant Flies

Cited by 81 publications

References 5 publications

Recognition and Detoxification of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1

Recognition and Detoxification of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1

PURIFICATION AND CHARACTERIZATION OF DDT-DEHYDROHALOGENASE FROMPseudomonas putidaT5

Inheritance of Ddt Resistance in a Laboratory Colony of the Housefly, Musca Domestica

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