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
4.1.3.40
-
RECOMMENDED NAME
GeneOntology No.
chorismate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chorismate = 4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-hydroxybenzoate biosynthesis II (bacteria and fungi)
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
ubiquinol-8 biosynthesis (eukaryotic)
-
Ubiquinone and other terpenoid-quinone biosynthesis
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
chorismate lyase
-
-
chorismate pyruvate-lyase
-
-
chorismate-pyruvate lyase
P26602
-
Rv2949c enzyme
-
-
CAS REGISTRY NUMBER
COMMENTARY
157482-18-3
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
a xanB2 deletion mutant exhibits a pleiotropic phenotype, including xanthomonadin deficiency, producing less exopolysaccharide, lower viability and H2O2 resistance, and lower virulence
malfunction
-
a xanB2 deletion mutant exhibits a pleiotropic phenotype, including xanthomonadin deficiency, producing less exopolysaccharide, lower viability and H2O2 resistance, and lower virulence
-
metabolism
-
the enzyme is a key metabolic enzyme linking xanthomonadin, coenzyme Q, and exopolysaccharide biosynthesis
metabolism
-
the enzyme is a key metabolic enzyme linking xanthomonadin, coenzyme Q, and exopolysaccharide biosynthesis
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
P26602
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
P26602
first step in ubiquinone biosynthesis
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
ubiquinone biosynthetic pathway
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
chorismate +
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no activity with 3-hydroxybenzoate and 4-hydroxybenzoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
P26602
first step in ubiquinone biosynthesis
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
ubiquinone biosynthetic pathway
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no activity with 3-hydroxybenzoate and 4-hydroxybenzoate
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
-
4-hydroxybenzaldehyde
-
-
4-hydroxybenzoate
-
product inhibition
4-hydroxybenzoate
-
strong product inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00197
-
chorismate
-
pH 7.5, 37C, recombinant enzyme produced in Mycobacterium smegmatis
0.0097
-
chorismate
-
pH 7.5, 37C
0.028
-
chorismate
-
pH 7.5, wild-type enzyme, initial rate analysis
0.029
-
chorismate
-
pH 7.5, wild-type enzyme, progress curve analysis
0.037
-
chorismate
-
pH 7.5, mutant enzyme C14S/C81S, initial rate analysis
0.039
-
chorismate
-
pH 7.5, mutant enzyme C14S/C81S, progress curve analysis
0.0396
-
chorismate
-
pH 7.5, 37C, recombinant enzyme produced in Escherichia coli
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.102
-
chorismate
-
pH 7.5, 37C, recombinant enzyme produced in Mycobacterium smegmatis
0.215
-
chorismate
-
pH 7.5, 37C, recombinant enzyme produced in Escherichia coli
0.82
-
chorismate
-
pH 7.5, 37C
1.3
-
chorismate
-
pH 7.5, mutant enzyme C14S/C81S, initial rate analysis
1.4
-
chorismate
-
pH 7.5, mutant enzyme C14S/C81S, progress curve analysis
1.5
-
chorismate
-
pH 7.5, wild-type enzyme, initial rate analysis
1.7
-
chorismate
-
pH 7.5, wild-type enzyme, progress curve analysis
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
pH 7.5, wild-type enzyme
0.33
-
4-hydroxybenzaldehyde
-
pH 7.5, wild-type enzyme
0.001
-
4-hydroxybenzoate
-
pH 7.5, 37C
0.0021
-
4-hydroxybenzoate
-
pH 7.5, wild-type enzyme
0.26
-
vanillate
-
pH 7.5, wild-type enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
expressed in hairy root cultures of Lithospermum erythrorhizon
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 18000, SDS-PAGE; x * 18776, calculation from nucleotide sequence
monomer
-
1 * 17000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, in presence of 10% glycerol the purified recombinant enzyme is stable for at least 3 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
wild-type and mutant enzyme C14S/C81S
-
recombinant enzyme produced in Escherichia coli and Mycobacterium smegmatis
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Lithospermum erythrorhizon under the control of the strong (ocs)3mas-promoter
-
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
-
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
-
production of recombinant enzyme in Escherichia coli and Mycobacterium smegmatis
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C14S/C81S
-
mutation causes greatly improved solution behavior and minor effect on enzyme activity
G90A
-
the KM-value for the substrate chorismate is unaffected, the Kp for the product is altered