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Chorismate lyase

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EC number
  
4.1.3.40

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
157482-18-3

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

Chorismate lyase

In enzymology, a chorismate lyase (EC 4.1.3.40) is an enzyme that catalyzes the chemical reaction

Contents

chorismate ⇌ 4-hydroxybenzoate + pyruvate

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.

Catalytic activity

  • Chorismate = 4HB + pyruvate
  • This enzyme has an optimum pH at 7.5

    • Enzymatic activity

    Inhibited by:

  • Vanillate
  • 4-hydroxybenzaldehyde
  • 3-carboxylmethylaminmethyl-4-hydroxybenzoic acid
  • 4HB - ubiC is inhibited by the product of the reaction, which scientists believe serves as a control mechanism for the pathway

    • 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.[1]

    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.

  • taxonomic lineage: bacteria → proteobacteria → gammaproteobacteria → enterobacteriales → enterobacteriaceae → escherichia → escherichia coli

    • Structure

    This enzyme is a monomer. Its secondary structure contains helixes, turns, and beta strands.

  • It has a mass of 18,777 daltons
  • Its sequence is 165 amino acids long

    • Binding Sites

  • position: 35(M)
  • position: 77(R)
  • position: 115(L)

    • Mutagenesis

  • position: 91- G → A; increases product inhibition by 40%. No effect on substrate affinity.
  • position: 156 - E → K; loss of activity

    • References

    Chorismate lyase Wikipedia
    (Text) CC BY-SA


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