Chorismate lyase

In enzymology, a chorismate lyase () is an enzyme that catalyzes the chemical reaction
Hence, this enzyme has one substrate, chorismate, and two products, 4-hydroxybenzoate and pyruvate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). Other names in common use include CL, CPL, and UbiC.
This enzyme catalyses the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in "Escherichia coli" and other Gram-negative bacteria. Its activity does not require metal cofactors.
Activity.
Enzymatic activity.
Inhibited by:
Pathway.
The pathway used is called the ubiquinone biosynthesis pathway, it catalyzes the first step in the biosynthesis of ubiquinone in "E. coli." Ubiquinone is a lipid-soluble electron-transporting coenzyme. They are essential electron carriers in prokaryotes and are essential in aerobic organisms to achieve ATP.
Nomenclature.
There are several different names for chorismate lyase. it is also called chorismate pyruvate lyase (4-hydroxybenzoate-forming) and it is also abbreviated several different ways: CPL, CL, and ubiC. It is sometimes referred to as ubiC, because that is the gene name. This enzyme belongs to the class Lyases; more specifically the ox-acid-lyase or the carbon-carbon-lyases.
Structure.
This enzyme is a monomer. Its secondary structure contains helixes, turns, and beta strands.