Chorismate lyase

Chorismate lyase
chorismate lyase with product, 1.0 a resolution
Identifiers
Symbol	Chor_lyase
Pfam	PF04345
Pfam clan	CL0122
InterPro	IPR007440
SCOP	1jd3
SUPERFAMILY	1jd3
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a chorismate lyase (EC 4.1.3.40) 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.

Inhibited by:

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.[1]

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.