Muconate lactonizing enzyme

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Muconate Lactonizing Enzyme[edit | edit source]

Crystal structure of Muconate Lactonizing Enzyme

Muconate lactonizing enzyme (MLE) is an important enzyme involved in the beta-ketoadipate pathway, a crucial metabolic route for the degradation of aromatic compounds in bacteria. This enzyme catalyzes the conversion of cis,cis-muconate to muconolactone, a key step in the breakdown of catechol and other aromatic compounds into simpler molecules that can be utilized as carbon sources by microorganisms.

Structure[edit | edit source]

Muconate lactonizing enzyme is a member of the enolase superfamily, characterized by a conserved active site architecture that facilitates the catalysis of a wide range of reactions. The enzyme typically functions as a homodimer, with each subunit contributing to the formation of the active site. The crystal structure of MLE, as shown in the image, reveals a complex folding pattern that is essential for its enzymatic activity.

Mechanism[edit | edit source]

The enzymatic mechanism of MLE involves the formation of an enolate intermediate. The enzyme stabilizes this intermediate through interactions with key residues in the active site, facilitating the cyclization of cis,cis-muconate to form muconolactone. This reaction is a crucial step in the degradation of aromatic compounds, allowing bacteria to utilize these compounds as energy sources.

Biological Role[edit | edit source]

Muconate lactonizing enzyme plays a vital role in the biodegradation of aromatic compounds, which are prevalent in the environment due to both natural and anthropogenic sources. By converting these compounds into forms that can be further metabolized, MLE helps in the detoxification and recycling of organic matter, contributing to the carbon cycle.

Industrial Applications[edit | edit source]

Due to its role in the degradation of aromatic compounds, MLE has potential applications in bioremediation processes. It can be used to clean up environments contaminated with aromatic pollutants, such as those found in petroleum and pesticides. The enzyme's ability to break down complex organic molecules makes it a valuable tool in environmental biotechnology.

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Contributors: Prab R. Tumpati, MD