Summary: Chorismate lyase
This is the Wikipedia entry entitled "Chorismate lyase". More...
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Chorismate lyase Edit Wikipedia article
|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
- 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 â†’ proteobacteria â†’ gammaproteobacteria â†’ enterobacteriales â†’ enterobacteriaceae â†’ escherichia â†’ 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 â†’ A; increases product inhibition by 40%. No effect on substrate affinity.
- position: 156 - E â†’ 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): 5309â€“16. 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 (Reading, Engl.) 140 (4): 897â€“904. doi:10.1099/00221287-140-4-897. PMID 8012607.
- Nichols BP, Green JM (1992). "Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase". J. Bacteriol. 174 (16): 5309â€“16. PMC 206367. PMID 1644758.
- Siebert M, Severin K, Heide L (Pt 4). "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase". Microbiology. 140 (4): 897â€“904. doi:10.1099/00221287-140-4-897. PMID 8012607. Check date values in:
- Meganathan R (2001). "Ubiquinone biosynthesis in microorganisms". FEMS. Microbiol. Lett. 203 (2): 131â€“9. doi:10.1111/j.1574-6968.2001.tb10831.x. PMID 11583838.
|This EC 4.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.|
Chorismate lyase Provide feedback
Chorismate lyase catalyses the first step in ubiquinone synthesis, i.e. the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate.
Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL; , Proteins 2001;44:304-311.: The crystal structure of chorismate lyase shows a new fold and a tightly retained product. PUBMED:11455603 EPMC:11455603
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007440
Chorismate--pyruvate lyase catalyses the first step in ubiquinone synthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria [PUBMED:1644758]. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine [PUBMED:11583838], however this enzyme is found only in bacteria. Its activity does not require metal cofactors [PUBMED:8012607].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||chorismate lyase activity (GO:0008813)|
|Biological process||ubiquinone biosynthetic process (GO:0006744)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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EGFdomains, and finally a single
- the UniProt description of the protein sequence
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Curation and family details
|Number in seed:||3|
|Number in full:||5653|
|Average length of the domain:||158.50 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||93.64 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Chor_lyase domain has been found. There are 11 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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