Information on EC 4.2.3.5 - chorismate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
4.2.3.5
-
RECOMMENDED NAME
GeneOntology No.
chorismate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with flavin reductase activity
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with diaphorase activity
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
stereochemistry
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with flavin reductase activity
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with flavin reductase activity
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
combination with flavin reductase activity
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
mechanism
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
show the reaction diagram
shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,4-trans elimination
-
-
1,4-trans elimination
-
-
1,4-trans elimination
-
-
1,4-trans elimination
-
-
beta-elimination
-
-
elimination
-
unusual 1,4-anti-elimination of the 3-phosphate group, enzyme is bifunctional
elimination
-
-
elimination
-
-
P-O bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chorismate biosynthesis from 3-dehydroquinate
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase (chorismate-forming)
Requires FMN. The reaction goes via a radical mechanism that involves reduced FMN and its semiquinone (FMNH(.)). Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-enolpyruvylshikimate-3-phosphate phospholyase
-
-
-
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate lyase
-
-
aroC
O15864
gene name
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
B5AAU3
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthase
C8Z2I6
gene Vlaro2
chorismate synthase
-
-
chorismate synthase
-
-
chorismate synthetase
-
-
-
-
EC 4.6.1.4
-
-
formerly
-
VEG216
-
-
-
-
Vegetative protein 216
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9077-07-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
methods of enzyme determination
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
-
C8Z2I6
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6S)-6-fluoro-5-enolpyruvylshikimate 3-phosphate
6-fluorochorismate + phosphate
show the reaction diagram
-
converion rate between 270 and 370 times slower than natural substrate conversion
-
-
?
(6S)-6-fluoro-5-enolpyruvylshikimate-3-phosphate
6-fluorochorismate + phosphate
show the reaction diagram
-
?
-
-
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
-
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
last enzyme of the shikimate pathway, catalyzes the anti-1,4-elimination of the 3-phosphate group and the C-(6proR) hydrogen from 5-enolpyruvylshikimate 3-phosphate
chorismate is a precursor for the biosynthesis of aromatic compounds
-
r
5-enolpyruvylshikimate-3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-O-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme of the shikimate pathway, catalyzes the NADH- and FMN-dependent synthesis of chorismate, a precursor of aromatic amino acids, naphthoquinones, menaquinones, and mycobactins
-
-
r
FMN + NADPH
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P31104
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P28777, -
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q12640
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-, P56122
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P27793
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
O66493
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q9WYI2, -
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
5-enolpyruvylshikimate 3-phosphate
-
ir
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
evidence for a radical mechanism
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
secondary beta deuterium kinetic isotope effect
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
enzyme of the shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q9WYI2, -
enzyme of the shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
enzyme is involved in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
last step in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
last step of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P31104
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q12640
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P27793
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P28777, -
seventh enzyme of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
the enzyme catalyzes the final step of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
FMN + NADPH
?
show the reaction diagram
-
recombinant enzyme has a diaphorase activity. NADPH binds in or near the substrate (O5-(1-carboxyvinyl)-3-phosphoshikimate) binding site, suggesting that NADPH binding to the enzyme is embedded in the general protein structure and a special NADPH binding domain is not required to generate the intrinsic oxidoreductase activity
-
?
additional information
?
-
P31104
enzyme has flavin reductase activity
-
?
additional information
?
-
-
enzyme shows flavin reductase activity
-
?
additional information
?
-
Q12640
enzyme shows flavin reductase activity
-
?
additional information
?
-
-
enzyme showsflavin reductase activity
-
?
additional information
?
-
Q9WYI2, -
monofunctional enzyme that does not have an intrinsic ability to reduce the FMN cofactor
-
?
additional information
?
-
-
monofunctional enzyme that does not possess an intrinsic flavin reductase activity
-
?
additional information
?
-
-
no flavin reductase activity
-
?
additional information
?
-
P27793
no flavin reductase activity
-
?
additional information
?
-
-
the enzyme also shows FMN:NADPH oxidoreductase activity
-
?
additional information
?
-
-
the dissociation constant for the S127A mutant protein is similar to that of the wild-type enzyme, whereas the replacement of S16 with alanine results in a slight increase of the dissociation constant
-
-
-
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
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
5-enolpyruvylshikimate 3-phosphate
chorismate + phosphate
show the reaction diagram
-
last enzyme of the shikimate pathway, catalyzes the anti-1,4-elimination of the 3-phosphate group and the C-(6proR) hydrogen from 5-enolpyruvylshikimate 3-phosphate
chorismate is a precursor for the biosynthesis of aromatic compounds
-
r
5-enolpyruvylshikimate-3-phosphate
chorismate + phosphate
show the reaction diagram
-
-
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-, P56122
-
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
enzyme of the shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q9WYI2, -
enzyme of the shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
enzyme is involved in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
last step in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
last step of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P31104
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
Q12640
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P27793
seventh enzyme in shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
P28777, -
seventh enzyme of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
the enzyme catalyzes the final step of shikimate pathway
-
?
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
?
show the reaction diagram
-
-
-
-
-
5-O-(1-carboxyvinyl)-3-phosphoshikimate
chorismate + phosphate
show the reaction diagram
-
seventh enzyme of the shikimate pathway, catalyzes the NADH- and FMN-dependent synthesis of chorismate, a precursor of aromatic amino acids, naphthoquinones, menaquinones, and mycobactins
-
-
r
additional information
?
-
-
the dissociation constant for the S127A mutant protein is similar to that of the wild-type enzyme, whereas the replacement of S16 with alanine results in a slight increase of the dissociation constant
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
Flavins
-
required, reduced forms e.g. FMN, FAD
-
FMN
Q9WYI2, -
cofactor
FMN
-
essential for catalytic activity
FMN
-
reduced, the S16A/S127A double-mutant protein showy slightly weaker binding of the cofactor
FMNH2
P28777
absolute requirement
FMNH2
-
absolute requirement for FMNH2, which is not consumed during the reaction
FMNH2
-, P56122
required. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar
FMNH2
P31104
absolute requirement, Km: 0.0125 mM
FMNH2
P27793
absolute requirement, Km: 37 nM
FMNH2
-
absolute requirement, Km: 76 nM
FMNH2
Q12640
absolute requirement, Km: 66 nM
FMNH2
-
absolute requirement, Km: 42 nM
FMNH2
-
absolute requirement
NADPH
-
required
FMNH2
-
absolute requirement, Km: 0.0048 mM
additional information
-
no activity with 5-deaza-FMN
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(3R,4R,5R)-5-(carboxymethoxy)-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
(3R,4S,5R)-4-hydroxy-3-[(2S)-1-hydroxy-1-oxo-2-phosphonooxypropan-2-yl]oxy-5-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
(3R,4S,5R)-5-(1-carboxyethoxy)-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
(3R,4S,5R)-5-[(1R)-1-carboxy-1-phosphonoethoxy]-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
(3R,4S,5S,6S)-5-(1-carboxyethenoxy)-6-fluoro-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
(6R)-6-fluoro-5-enoylpyruvylshikimate 3-phosphate
-
IC50 is 0.0005 mM when the enzyme is preincubated with the inhibitor, the IC50 is 0.25 mM when the enzyme is not preincubated with the inhibitor, inhibition is not absolutely irreversible
(6S)-6-fluoro-5-enolpyruvylshikimate 3-phosphate
-
competitive inhibitor
2-difluoro-[1-phosphonooxyethoxy]-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
-
-
bathophenanthroline
-
-
diethyl dicarbonate
-
-
dioxygen
-
inactivation
O2
-
activity only in anaerobic conditions
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
light
-
stimulation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0027
-
5-enolpyruvylshikimate 3-phosphate
-
wild-type enzyme
0.011
-
5-enolpyruvylshikimate 3-phosphate
-
isozyme MatCS1
0.0127
-
5-enolpyruvylshikimate 3-phosphate
-
-
0.027
-
5-enolpyruvylshikimate 3-phosphate
-
-
0.047
-
5-enolpyruvylshikimate 3-phosphate
-
-
0.08
-
5-enolpyruvylshikimate 3-phosphate
-
isozyme MatCS2
0.043
-
NADPH
-
FMN:NADPH oxidoreductase activity, wild-type enzyme
0.11
-
NADPH
-
FMN:NADPH oxidoreductase activity, mutant enzyme H17A
0.28
-
NADPH
-
FMN:NADPH oxidoreductase activity, mutant enzyme H106A
0.0013
0.0022
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
-
0.0027
0.007
O5-(1-carboxyvinyl)-3-phosphoshikimate
Q12640
-
0.0097
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
-
0.011
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
enzyme form CS1
0.0127
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
-
0.027
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
-
0.053
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
P27793
-
0.08
-
O5-(1-carboxyvinyl)-3-phosphoshikimate
-
enzyme form CS2
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
5-enolpyruvylshikimate 3-phosphate
-
mutant S16A
0.14
-
5-enolpyruvylshikimate 3-phosphate
-
mutant S127A
0.87
-
5-enolpyruvylshikimate 3-phosphate
-
wild-type enzyme
0.0083
-
NADH
-
kinetics of reduction of the MtCS-bound FMNox is determined using fixed amount of holoenzyme and varying levels of NADH
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00179
-
(3R,4R,5R)-5-(carboxymethoxy)-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
0.000109
-
(3R,4S,5R)-4-hydroxy-3-[(2S)-1-hydroxy-1-oxo-2-phosphonooxypropan-2-yl]oxy-5-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
0.000192
-
(3R,4S,5R)-5-(1-carboxyethoxy)-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
0.000526
-
(3R,4S,5R)-5-[(1R)-1-carboxy-1-phosphonoethoxy]-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
0.000815
-
(3R,4S,5S,6S)-5-(1-carboxyethenoxy)-6-fluoro-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
0.00061
-
2-difluoro-[1-phosphonooxyethoxy]-4-hydroxy-3-phosphonooxycyclohexene-1-carboxylic acid
O15864, -
theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
(6R)-6-fluoro-5-enoylpyruvylshikimate 3-phosphate
-
IC50 is 0.0005 mM when the enzyme is preincubated with the inhibitor, the IC50 is 0.25 mM when the enzyme is not preincubated with the inhibitor, inhibition is not absolutely irreversible
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.004
-
-
CS activity
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
bifunctionality is determined by measurements of both chorismate synthase and NADH:FMN oxidoreductase activities; in the presence of oxygen the CS activity is limited by the reoxidation of FMNred cofactor
additional information
-
-
activity of mutant S127A is 6fold lower than that of the wild-type protein; activity of mutant S16A is 70fold lower than that of the wild-type protein; chorismate synthase has an intrinsic NADPH: FMN oxidoreductase activity that enables the enzyme to generate the reduced FMN cofactor (bifunctionality); no activity of double-mutant protein S16A/S127A, replacement of both serine residues produces a synergistic effect
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
enzyme form CS1; enzyme form CS2
6.5
8.5
-
-
7
8.5
Q12640
-
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at, CS activity and FMN-reductase activity
25
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
Q12640
-
5.5
-
P31104
-
6.8
-
O15864, -
calculated
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41800
-
-
determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis and electrospray mass spectrometry
80100
-
-
gel filtration
110000
138000
-
gel filtration
110000
-
-
sucrose density gradient centrifugation
144000
-
-
gel filtration after cross-linkage with dimethyl suberimidate
186800
-
-
gel filtration
190000
-
-
nondenaturing PAGE
198000
-
-
gel filtration after cross-linkage with dimethyl suberimidate
198000
-
-
dynamic light scattering analysis
200000
-
Q9WYI2, -
non-denaturing PAGE in presence of O5-(1-carboxyvinyl)-3-phosphoshikimate and FMN
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 41700
?
O15864, -
x * 59000, calculated
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 41900, SDS-PAGE
dimer
P27793
2 * 41771
dimer
Q12640
2 * 46400, dimer or tetramer
dimer
-
2 * 40800, dimer or tetramer
dimer
-
2 * 41605, dimer or tetramer, enzyme form CS2; 2 * 41902, dimer or tetramer, enzyme form CS1
dimer
-
analytical ultracentrifugation, low equilibrium between dimer and tetramer
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 43024, electrospray mass spectrometry
tetramer
Q9WYI2, -
4 * 41754, calculation from amino acid sequence; 4 * 42000, SDS-PAGE
tetramer
-
4 * 39138
tetramer
Q12640
4 * 46400, dimer or tetramer
tetramer
-
4 * 40800, dimer or tetramer
tetramer
-
4 * 41605, dimer or tetramer, enzyme form CS2; 4 * 41902, dimer or tetramer, enzyme form CS1
tetramer
-
4 * 43026
tetramer
-
crystallization data, low equilibrium between dimer and tetramer
tetramer
-
-
trimer
P31104
heterotrimer
dimer
-
in solution, determined by gel filtration chromatography
additional information
-
x * 40000, SDS-PAGE
additional information
-
x * 24000, SDS-PAGE
additional information
-
x * 41700, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
P27793
the precursor protein has a MW of 47722 Da
proteolytic modification
-
the precursor protein has a MW of 46871, enzyme form CS2; the precursor protein has a MW of 47722, enzyme form CS1
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of the enzyme reveals a novel beta alpha beta sandwich topology
O66493
crystal structure of chorismate synthase in both FMN-bound and FMN-free form. It is a tetrameric enzyme, with each monomer possessing a novel beta-alpha-beta sandwich fold
-, P56122
hanging-drop vapour-diffusion method, crystallization at 296 K using polyethylene glycol 400 as precipitant, recombinant enzyme fused with an eight-residue C-terminal tag
-
beta-alpha-beta sandwich structure
-
homology modeling of structure of chorismate synthase along with cofactor FMN using crystal structure of Helicobacter pylori chorismate synthase. Each monomer of Plasmodium falciparum chorismate synthase consists of 10 helices and 13 sheets. The core of monomer has a unique beta-alpha-beta sandwich fold that appears as a three layered structure in the predicted model. This unique fold consists of two antiparallel five stranded beta-sheet layers and four alpha-helices which are sandwiched between these two beta-sheet layers. The unique beta-alpha-beta-sandwich provides a scaffold for cofactor and substrate binding. The residues involved in polar interactions with substrate 5-enolpyruvylshikimate-3-phosphate are Arg46, Lys60, Asp61, Lys90, Ser121, Ser122 and Arg491
O15864, -
hanging drop vapour diffusion method, three-dimensional X-ray structure from selenomethionine-labeled crystals at 2.2 A resolution. The structure shows a novel beta,alpha,beta,alpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers. The molecule is arranged as a tight tetramer with D2 symmetry
P28777
hanging-drop vapour diffusion method. Crystal streucture solved at 1.0 A
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
92
-
Q9WYI2, -
melting temperature above
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
apparent stability of all mutant proteins is comparable to that of the wild-type enzyme
-
bovine serum albumin stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.05 mM Tris-HCl, pH 7.5, 0.01 mM FMN, 10% glycerol, 3 mM mercaptoethanol, 4 months
-
4C, 2 weeks
-
-15C, several months
-
-20C, 50 mM Tris-HCl buffer, pH 7.5, 0.4 mM dithiothreitol, 50% glycerol
-
-15C, 0.1 M potassium phosphate buffer, pH 7.0, 0.1 mM EDTA, 0.2 mM dithiothreitol, more than 6 months
-
-20C, 50 mM Tris-HCl buffer, pH 7.5, 0.4 mM dithiothreitol, 50% glycerol
-
liquid nitrogen
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
together with NADPH dependent flavin reductase
-
expressed in Escherichia coli
-
recombinant enzyme fused with an eight-residue C-terminal tag
-
by using a 3-step purification (anion exchange, hydrophobic interaction and anion exchange chromatography)
-
by two-step chromatographic procedure
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
recombinant enzyme
Q9WYI2, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
expression in Escherichia coli
-
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli, fused with an eight-residue C-terminal tag
-
-
B5AAU3, -
cloning and expression in Escherichia coli strain Rosetta(DE3) in the absence of IPTG induction, heterologous overexpression of the MtCS protein
-
expression in Escherichia coli
-
mutant proteins are heterologously expressed in Escherichia coli, strain BL21(DE3)RP
-
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
expression in Escherichia coli
Q9WYI2, -
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
expressed in Saccharomyces cerevisiae
C8Z2I6, -
expression in a chorismate synthase deficient Saccharomyces cerevisiae strain
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D367A
-
comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower
D367N
-
comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower
H106A
-
mutant enzyme with 20fold reduced activity
H106A
-
activity 10fold decreased
H17A
-
mutant enzyme with 10fold reduced activity
H17A
-
activity 20fold decreased
S127A
-
amino acid replacements are performed using the QuikChange site-directed mutagenesis kit
S16A
-
amino acid replacements are performed using the QuikChange site-directed mutagenesis kit
S16A/S127A
-
double-mutant protein
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
enzymes of shikimate pathway are attractive targets to the development of antitubercular agents