DDT-dehydrochlorinase
DDT-dehydrochlorinase is an enzyme that catalyzes the chemical reaction of 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane, also known as DDT, into 1,1-dichloro-2,2-bis(4-chlorophenyl)ethene. This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds.
Function[edit | edit source]
DDT-dehydrochlorinase plays a crucial role in the metabolism of DDT, a synthetic insecticide that has been widely used in agriculture and public health. The enzyme is responsible for the dehydrochlorination of DDT, a key step in the degradation of this persistent organic pollutant.
Structure[edit | edit source]
The structure of DDT-dehydrochlorinase is not fully understood. However, like other enzymes, it is likely to have an active site where the substrate (DDT) binds and a catalytic site where the reaction takes place.
Biological Role[edit | edit source]
DDT-dehydrochlorinase is found in various organisms, including bacteria and fungi, that are capable of degrading DDT. The enzyme is part of the metabolic pathway that these organisms use to break down DDT and use it as a source of energy.
Clinical Significance[edit | edit source]
Understanding the function and mechanism of DDT-dehydrochlorinase is important for the development of bioremediation strategies to clean up DDT-contaminated environments. The enzyme could potentially be used in engineered bacteria or fungi to accelerate the degradation of DDT in polluted soils or waters.
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References[edit | edit source]
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Contributors: Prab R. Tumpati, MD