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Information on EC 4.1.3.40 - chorismate lyase and Organism(s) Escherichia coli and UniProt Accession P26602
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4.1.3.40 chorismate lyaseIUBMB Comments
This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria . The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine .
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
chorismate pyruvate-lyase, chorismate lyase, xanb2, chorismate-pyruvate lyase, sll1797, rv2949c enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
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
157482-18-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chorismate
4-hydroxybenzoate + pyruvate
first step in ubiquinone biosynthesis
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
-
ubiquinone biosynthetic pathway
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chorismate
4-hydroxybenzoate + pyruvate
first step in ubiquinone biosynthesis
-
-
?
chorismate
4-hydroxybenzoate + pyruvate
-
ubiquinone biosynthetic pathway
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expressed in hairy root cultures of Lithospermum erythrorhizon
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme expression improves coenzyme Q10 production in Saccharomyces pombe 2fold
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G90A
the KM-value for the substrate chorismate is unaffected, the Kp for the product is altered
C14S/C81S
-
mutation causes greatly improved solution behavior and minor effect on enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nichols, B.P.; Green, J.M.
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase
J. Bacteriol.
174
5309-5316
1992
Escherichia coli (P26602), Escherichia coli
Holden, M.J.; Mayhew, M.P.; Gallagher, D.T.; Vilker, V.L.
Chorismate lyase: kinetics and engineering for stability
Biochim. Biophys. Acta
1594
160-167
2002
Escherichia coli
Gallagher, D.T.; Mayhew, M.; Holden, M.J.; Howard, A.; Kim, K.J.; Vilker, V.L.
The crystal structure of chorismate lyase shows a new fold and a tightly retained product
Proteins
44
304-311
2001
Escherichia coli (P26602), Escherichia coli
Smith, N.; Roitberg, A.E.; Rivera, E.; Howard, A.; Holden, M.J.; Mayhew, M.; Kaistha, S.; Gallagher, D.T.
Structural analysis of ligand binding and catalysis in chorismate lyase
Arch. Biochem. Biophys.
445
72-80
2006
Escherichia coli (P26602), Escherichia coli
Siebert, M.; Bechthold, A.; Melzer, M.; May, U.; Berger, U.; Schroder, G.; Schroder, J.; Severin, K.; Heide, L.
Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli
FEBS Lett.
307
347-350
1992
Escherichia coli
Khle, A.; Sommer, S.; Yazaki, K.; Ferrer, A.; Boronat, A.; Li, S.M.; Heide, L.
High level expression of chorismate pyruvate-lyase (UbiC) and HMG-CoA reductase in hairy root cultures of Lithospermum erythrorhizon
Plant Cell Physiol.
43
894-902
2002
Escherichia coli
Siebert, M.; Sommer, S.; Li, S.M.; Wang, Z.X.; Severin, K.; Heide, L.
Genetic engineering of plant secondary metabolism. Accumulation of 4-hydroxybenzoate glucosides as a result of the expression of the bacterial ubiC gene in tobacco
Plant Physiol.
112
811-819
1996
Escherichia coli
Viitanen, P.V.; Devine, A.L.; Khan, M.S.; Deuel, D.L.; Van Dyk, D.E.; Daniell, H.
Metabolic engineering of the chloroplast genome using the Escherichia coli ubiC gene reveals that chorismate is a readily abundant plant precursor for p-hydroxybenzoic acid biosynthesis
Plant Physiol.
136
4048-4060
2004
Escherichia coli
Moriyama, D.; Hosono, K.; Fujii, M.; Washida, M.; Nanba, H.; Kaino, T.; Kawamukai, M.
Production of CoQ10 in fission yeast by expression of genes responsible for CoQ10 biosynthesis
Biosci. Biotechnol. Biochem.
79
1026-1033
2015
Escherichia coli
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