Enzymes
UniProtKB help_outline | 8 proteins |
Enzyme class help_outline |
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GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane Identifier CHEBI:16130 (Beilstein: 1882657; CAS: 50-29-3) help_outline Charge 0 Formula C14H9Cl5 InChIKeyhelp_outline YVGGHNCTFXOJCH-UHFFFAOYSA-N SMILEShelp_outline Clc1ccc(cc1)C(c1ccc(Cl)cc1)C(Cl)(Cl)Cl 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene Identifier CHEBI:16598 (CAS: 72-55-9) help_outline Charge 0 Formula C14H8Cl4 InChIKeyhelp_outline UCNVFOCBFJOQAL-UHFFFAOYSA-N SMILEShelp_outline ClC(Cl)=C(C1=CC=C(Cl)C=C1)C1=CC=C(Cl)C=C1 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline chloride Identifier CHEBI:17996 (Beilstein: 3587171; CAS: 16887-00-6) help_outline Charge -1 Formula Cl InChIKeyhelp_outline VEXZGXHMUGYJMC-UHFFFAOYSA-M SMILEShelp_outline [Cl-] 2D coordinates Mol file for the small molecule Search links Involved in 139 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:19217 | RHEA:19218 | RHEA:19219 | RHEA:19220 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae.
Ranson H., Prapanthadara L., Hemingway J.
Two cDNA species, aggst1-5 and aggst1-6, comprising the entire coding region of two distinct glutathione S-transferases (GSTs) have been isolated from a 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) resistant strain (ZANDS) of Anopheles gambiae. The nucleotide sequences of these cDNA specie ... >> More
Two cDNA species, aggst1-5 and aggst1-6, comprising the entire coding region of two distinct glutathione S-transferases (GSTs) have been isolated from a 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) resistant strain (ZANDS) of Anopheles gambiae. The nucleotide sequences of these cDNA species share 80.2% identity and their derived amino acid sequences are 82.3% similar. They have been classified as insect class I GSTs on the basis of their high sequence similarity to class I GSTs from Drosophila melanogaster and Musca domestica and they are localized to a region of an An. gambiae chromosome known to contain further class I GSTs. The genes aggst1-5 and aggst1-6 were expressed at high levels in Escherichia coli and the recombinant GSTs were purified by affinity chromatography and characterized. Both agGST1-5 and agGST1-6 showed high activity with the substrates 1-chloro-2,4-dinitrobenzene and 1, 2-dichloro-4-nitrobenzene but negligible activity with the mammalian theta class substrates, 1,2-epoxy-3-(4-nitrophenoxy)propane and p-nitrophenyl bromide. Despite their high level of sequence identity, agGST1-5 and agGST1-6 displayed different kinetic properties. Both enzymes were able to metabolize DDT and were localized to a subset of GSTs that, from earlier biochemical studies, are known to be involved in insecticide resistance in An. gambiae. This subset of enzymes is one of three in which the DDT metabolism levels are elevated in resistant insects. << Less
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Recognition and detoxification of the insecticide DDT by Drosophila melanogaster glutathione S-transferase D1.
Low W.Y., Feil S.C., Ng H.L., Gorman M.A., Morton C.J., Pyke J., McConville M.J., Bieri M., Mok Y.F., Robin C., Gooley P.R., Parker M.W., Batterham P.
GSTD1 is one of several insect glutathione S-transferases capable of metabolizing the insecticide DDT. Here we use crystallography and NMR to elucidate the binding of DDT and glutathione to GSTD1. The crystal structure of Drosophila melanogaster GSTD1 has been determined to 1.1 A resolution, which ... >> More
GSTD1 is one of several insect glutathione S-transferases capable of metabolizing the insecticide DDT. Here we use crystallography and NMR to elucidate the binding of DDT and glutathione to GSTD1. The crystal structure of Drosophila melanogaster GSTD1 has been determined to 1.1 A resolution, which reveals that the enzyme adopts the canonical GST fold but with a partially occluded active site caused by the packing of a C-terminal helix against one wall of the binding site for substrates. This helix would need to unwind or be displaced to enable catalysis. When the C-terminal helix is removed from the model of the crystal structure, DDT can be computationally docked into the active site in an orientation favoring catalysis. Two-dimensional (1)H,(15)N heteronuclear single-quantum coherence NMR experiments of GSTD1 indicate that conformational changes occur upon glutathione and DDT binding and the residues that broaden upon DDT binding support the predicted binding site. We also show that the ancestral GSTD1 is likely to have possessed DDT dehydrochlorinase activity because both GSTD1 from D. melanogaster and its sibling species, Drosophila simulans, have this activity. << Less