Information on EC 4.1.3.40 - chorismate lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.3.40
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RECOMMENDED NAME
GeneOntology No.
chorismate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chorismate = 4-hydroxybenzoate + pyruvate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxybenzoate biosynthesis II (microbes)
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Biosynthesis of secondary metabolites
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Metabolic pathways
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p-HBAD biosynthesis
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phenolphthiocerol biosynthesis
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tetrahydromethanopterin biosynthesis
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ubiquinol-8 biosynthesis (eukaryotic)
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Ubiquinone and other terpenoid-quinone biosynthesis
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ubiquinone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
chorismate pyruvate-lyase (4-hydroxybenzoate-forming)
This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria [1]. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine [3].
CAS REGISTRY NUMBER
COMMENTARY hide
157482-18-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
chorismate +
4-hydroxybenzoate + pyruvate
show the reaction diagram
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?
additional information
?
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no activity with 3-hydroxybenzoate and 4-hydroxybenzoate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
additional information
?
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no activity with 3-hydroxybenzoate and 4-hydroxybenzoate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-carboxymethylaminomethyl-4-hydroxybenzoate
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4-hydroxybenzaldehyde
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4-hydroxybenzoate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00197 - 0.0396
chorismate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.102 - 1.7
chorismate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
3-carboxymethylaminomethyl-4-hydroxybenzoate
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pH 7.5, wild-type enzyme
0.33
4-hydroxybenzaldehyde
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pH 7.5, wild-type enzyme
0.001 - 0.0021
4-hydroxybenzoate
0.26
vanillate
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pH 7.5, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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expressed in hairy root cultures of Lithospermum erythrorhizon
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the recombinant enzyme shows severalfold higher specific activities in membrane than in soluble protein fractions
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 18000, SDS-PAGE; x * 18776, calculation from nucleotide sequence
monomer
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1 * 17000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.0 A crystal structure of the enzyme-product complex, 2.0 A structure of the G90A mutant enzyme with bound product, 2.4 A structure of the enzyme complexed with the inhibitor vanillate, 1.9 A structure of the G90A mutant enzyme with the inhibitor vanillate
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structure of wild-type enzyme, mutant enzyme C14S and C14S/C81S in enzyme-product complex. Structure is determined by heavy atom methods using the single mutant in its orthorhombic crystal form, and subsequently solved by molecular replacement in both the wild-type and double-mutant forms
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, in presence of 10% glycerol the purified recombinant enzyme is stable for at least 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme produced in Escherichia coli and Mycobacterium smegmatis
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recombinant GST-tagged enzyme from Escherichia coli strain BL21AI by glutathione affinity chromatography
wild-type and mutant enzyme C14S/C81S
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Lithospermum erythrorhizon under the control of the strong (ocs)3mas-promoter
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expression in Nicotiana tabacum under control of the constitutive plant promoter. The gene product is targeted into the plastid by fusing it to the sequence for the chloroplast transit peptide of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Transgenic plants show high chorismate pyruvate-lyase activity and accumulate 4-hydroxybenzoate as beta-glucosides, with the glucose attached to either the hydroxy or the carboxyl function of 4-hydroxybenzoate. The total content of 4-hydroxybenzoate glucosides is approximately 0.52% of dry weight, which exceeds the content of untransformed plants by at least a factor of 1000
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gene sll1797, phylogenetic analysis and tree, expression in Escherichia coli strain BL21AI as GST-tagged protein, and in Escherichia coli strain BW25113 for quantitative expression analysis by real time quantitative PCR. Complementation of ubiquinone-deficient Escherichia coli mutants by catalytic activity of heterologous Sll1797
production of recombinant enzyme in Escherichia coli and Mycobacterium smegmatis
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the ubiC gene is integrated into the chloroplast genome of Nicotiana tabacum under the control of the light-regulated psbA 5'-untranslated region. the limitation for 4-hydroxybenzoate production in nuclear-transformed plants is the activity of chorismate pyruvate-lyase activity. The process becomes substrate-limited only when the enzyme is present at very high levels in the compartment of interest
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C14S/C81S
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mutation causes greatly improved solution behavior and minor effect on enzyme activity
G90A
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the KM-value for the substrate chorismate is unaffected, the Kp for the product is altered
additional information
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