Catechol dioxygenase

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Catechol Dioxygenase[edit | edit source]

The reaction catalyzed by catechol dioxygenase.

Catechol dioxygenase is an enzyme that plays a crucial role in the degradation of aromatic compounds in various microorganisms. It is involved in the initial step of the catechol degradation pathway, which is responsible for the breakdown of aromatic compounds such as benzene, toluene, and xylene.

Structure[edit | edit source]

Catechol dioxygenase is a protein enzyme that is typically composed of multiple subunits. The exact structure and composition of the enzyme can vary depending on the specific microorganism it is found in. However, most catechol dioxygenases consist of an iron-containing active site, which is responsible for the catalytic activity of the enzyme.

Function[edit | edit source]

The primary function of catechol dioxygenase is to catalyze the conversion of catechol to muconic acid. This reaction involves the insertion of molecular oxygen into the catechol molecule, resulting in the formation of a cyclic intermediate. This intermediate is then further processed to produce muconic acid, which can be further metabolized by downstream enzymes.

Catechol dioxygenase is an essential enzyme in the degradation of aromatic compounds because it allows microorganisms to utilize these compounds as a source of carbon and energy. By breaking down aromatic compounds, microorganisms can effectively remove these pollutants from the environment.

Role in Bioremediation[edit | edit source]

Due to its ability to degrade aromatic compounds, catechol dioxygenase has significant applications in bioremediation. Bioremediation is a process that uses microorganisms to remove pollutants from contaminated environments. Catechol dioxygenase, along with other enzymes involved in the catechol degradation pathway, can be utilized to enhance the degradation of aromatic compounds in contaminated soil or water.

References[edit | edit source]


See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD