|PDB structures||RCSB PDB PDBe PDBsum|
- chorismate 4-hydroxybenzoate + 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.
chorismate lyase with product, 1.0 a resolution
|SCOPe||1jd3 / SUPFAM|
- Chorismate = 4HB + pyruvate
- This enzyme has an optimum pH at 7.5
- 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
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.
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
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
- position: 35(M)
- position: 77(R)
- position: 115(L)
- position: 91- G → A; increases product inhibition by 40%. No effect on substrate affinity.
- position: 156 - E → K; loss of activity
- Nichols BP, Green JM (August 1992). "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase". J. Bacteriol. 174 (16): 5309–16. doi:10.1128/jb.174.16.5309-5316.1992. PMC 206367. PMID 1644758.
- Siebert M, Severin K, Heide L (April 1994). "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase". Microbiology. 140 (4): 897–904. doi:10.1099/00221287-140-4-897. PMID 8012607.
- "UniprotID: P26602".
- "EC 188.8.131.52".
- Nichols BP, Green JM (1992). "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase". J. Bacteriol. 174 (16): 5309–16. doi:10.1128/jb.174.16.5309-5316.1992. PMC 206367. PMID 1644758.
- Siebert M, Severin K, Heide L (1994). "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase". Microbiology. 140 (4): 897–904. doi:10.1099/00221287-140-4-897. PMID 8012607.
- Meganathan R (2001). "Ubiquinone biosynthesis in microorganisms". FEMS Microbiol. Lett. 203 (2): 131–9. doi:10.1111/j.1574-6968.2001.tb10831.x. PMID 11583838.
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