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Information on EC 2.5.1.19 - 3-phosphoshikimate 1-carboxyvinyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A6D3
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EC Tree
2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferaseSpecify your search results
Word Map
- 2.5.1.19
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excitatory
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postsynaptic
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depolarization
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ipsps
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afferent
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monosynaptic
- hippocampal
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pyramidal
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presynaptic
- synapses
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latency
-
fire
- nmda
- motoneuron
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interneurons
- glyphosate
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firing
-
hyperpolarization
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electrophysiological
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antidromic
-
summation
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subthreshold
- bicuculline
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gabaa
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disynaptic
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non-nmda
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tetanic
-
6-cyano-7-nitroquinoxaline-2,3-dione
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volley
-
schaffer
-
quantal
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unitary
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paired-pulse
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orthodromic
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glyphosate-resistant
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short-latency
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thalamocortical
- biotechnology
-
electrotonic
-
reticulospinal
- radiatum
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homonymous
- drug development
- agriculture
- synthesis
-
interstimulus
-
funiculus
-
suprathreshold
-
preganglionic
-
low-threshold
-
impale
-
decerebrate
- biocytin
-
afterhyperpolarization
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
epsps, 5-enolpyruvylshikimate-3-phosphate synthase, epsp synthase, cp4 epsps, mepsps, 5-enolpyruvylshikimate 3-phosphate synthase, 5-enol-pyruvylshikimate-3-phosphate synthase, caepsps, 5-enol-pyruvyl-shikimate-3-phosphate synthase, 3-phosphoshikimate 1-carboxyvinyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-enolpyruvylshikimate 3-phosphate synthase
5-enolpyruvylshikimate-3-phosphate synthase
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3-enolpyruvylshikimate 5-phosphate synthase
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-
-
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3-enolpyruvylshikimic acid-5-phosphate synthetase
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-
-
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5'-enolpyruvylshikimate-3-phosphate synthase
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-
-
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5-enolpyruvyl-3-phosphoshikimate synthase
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-
-
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5-enolpyruvylshikimate-3-phosphate synthase
5-enolpyruvylshikimate-3-phosphate synthetase
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-
-
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5-enolpyruvylshikimate-3-phosphoric acid synthase
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-
-
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5-enolpyruvylshikimic acid-3-phosphate synthase
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-
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enolpyruvylshikimate phosphate synthase
-
-
-
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EPSP synthase
synthase, 5-enolpyruvoylshikimate 3-phosphate
-
-
-
-
additional information
enzyme belongs to the family of enolpyruvyl transferases
5-enolpyruvylshikimate 3-phosphate synthase
class I, glyphosate-sensitive
5-enolpyruvylshikimate-3-phosphate synthase
-
-
-
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EPSP synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
binding of shikimate 3-phosphate leads to a saturable and stable conformational change in the isolated N-terminal domain
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
catalytic mechanism, tetrahedral reaction intermediate, active site structure, wild-type and mutant D313A
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
catalytic mechanism, tetrahedral reaction intermediate, catalytic cycle of the enzyme, overview
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
via formation of a tetrahedral intermediate (TI) after which residue His385 is in a neutral form while residues Lys22, Lys340 and Lys411 are protonated, Asp313 mediates attack of the TI C4-OH group (as oxyanion, shikimate-3-phosphate moiety) at the TI C3-methyl group (phosphoenolpyruvate moiety), Lys22 serves as general acid catalyst for TI breakdown
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
proposed mechanism
-
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
enolpyruvylshikimate 3-phosphate ketal is catalytically formed as side product upon enolpyruvyl activation through protonation by an intramolecular nucleophilic addition of O4 to C2 of the enolpyruvyl moiety
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
enolpyruvate group transfer
induced-fit mechanism, formation of a 2-(S) configured tetrahedral reaction intermediate by covalent linkage of the two substrates
enolpyruvate group transfer
enolpyruvate group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:3-phosphoshikimate 5-O-(1-carboxyvinyl)-transferase
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CAS REGISTRY NUMBER
COMMENTARY
9068-73-9
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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
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
via formation of a 2-(S)-tetrahedral reaction intermediate (TI), pH 7.5, 25°C, 30 min
examination by malachite green phosphate-release assay
-
?
5-enolpyruvylshikimate 3-phosphate + H2O
5-enolpyruvylshikimate 3-phosphate ketal
-
enzymatic hydrolysis, pH 7.0, 25°C, in presence of phosphate scavenging system and excess of enzyme
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
-
enolpyruvylshikimate 3-phosphate ketal formation from shikimate 3-phosphate (radiolabelled) and phosphoenolypyruvate (in excess over shikimate 3-phosphate) by hydrolysis of product 5-enpolpyruvylshikimate 3-phosphate in presence of 25% excess of enzyme, pH 7.0, 25°C
analysis of products by ion-paired C18 reverse-phase HPLC and scintillation counting
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
6th enzyme in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
penultimate step in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
substrate binding of wild-type and mutant D313A, overview
-
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
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detection of inorganic phosphate by reaction with Lanzetta reagent and change in optical density at 660 nm
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
30 min, 25°C, pH 7.5, in presence of 2 mM dithiothreitol
detection of phosphate generation with Lanzetta reagent and change in absorbance at 650 nm
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
transfers enolpyruvate group from phosphoenolpyruvate to 5-hydroxyl group of 3-phosphoshikimate
i.e. 5-O-(1-carboxyvinyl)-3-phosphoshikimate
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
sixth reaction of chorismate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in chorismate biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in aromatic acid biosynthesis
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-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
key enzyme in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
the enzyme must promote breakdown of enolpyruvylshikimate 3-phosphate though enolpyruvyl activation, forming either the enolpyruvylshikimate 3-phosphate cation or a highly cation-like transition state
-
-
?
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
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
6th enzyme in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
penultimate step in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
sixth reaction of chorismate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in chorismate biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in aromatic acid biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
key enzyme in the shikimate pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
RP-TI, (R)-phosphonate analogue of the (S)-tetrahedral reaction intermediate, very potent competitive inhibitor of EPSPS forward reaction, binding induces substantial conformational change in enzymes backbone and active site (e.g., Glu341 and Arg124)
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
SP-TI, (S)-phosphonate analogue of the (S)-tetrahedral reaction intermediate, moderate competitive inhibitor of EPSPS forward reaction
(3R,4S,5R)-5-((R)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid
analogue of the tetrahedral reaction intermediate, competitive to both substrates, binding structure analysis, binding induces conformational changes to residues Arg124 and Glu341 within the active site, which results in structural alterations in the amino-terminal globular domain of the enzyme
(3R,4S,5R)-5-((S)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid
analogue of the tetrahedral reaction intermediate, competitive to both substrates, binding structure analysis, binding induces no conformational changes
(3R,4S,5R)-5-[(2R)-1,1-difluoro-3-hydroxy-3-oxo-2-phosphonooxy-propan-2-yl]oxy-4-hydroxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
2F-TI, (R)-difluoromethyl analogue of the (S)-tetrahedral reaction intermediate, very potent competitive inhibitor of EPSPS forward reaction
(Z)-3-fluorophosphoenolpyruvate
-
competitive vs. phosphoenolpyruvate at saturated shikimate 3-phosphate concentration and vice versa
3-Bromopyruvate
-
0.1 mM, approx. 80% inactivation after 5 min, maximum rate-constant: 0.31/min, substrates or a combination of shikimate 3-phosphat and glyphosate protect from inactivation, bromopyruvate modifies residues C408 and L411
diethyldicarbonate
-
inactivation with a second-order rate constant of 220/M/min, subtstrates protect from inactivation, enzyme activity is recovered by treatment with hydroxylamine
glyphosate
-
competitive inhibition of the wild-type enzyme, mutant T42M is less sensitive
pyruvate
-
20 mM, 85% inactivation after 1 h in the presence of cyanoborhydride, no inactivation in the absence of cyanoborhydride, preincubation with 5-enolpyruvylshikimate or a combination of shikimate 3-phosphate and glyphosate prevents from inactivation
N-phosphonomethylglycine
-
-
N-phosphonomethylglycine
-
inhibition of enolpyruvate transfer, competitive vs. phosphoenolpyruvate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
phosphoenolpyruvate
mutant G96A/A183T, in presence of 1 mM shikimate 3-phosphate
3.1
phosphoenolpyruvate
mutant G96A, in presence of 1 mM shikimate 3-phosphate
3.8
phosphoenolpyruvate
mutant A183T, in presence of 1 mM shikimate 3-phosphate
0.003
5-enolpyruvylshikimate 3-phosphate
-
recombinant overproducing strain
additional information
additional information
stopped-flow kinetics
-
additional information
additional information
small residue substitutions for Pro101 do not alter the KM for phosphoenolpyruvate and shikimate 3-phosphate
-
additional information
additional information
-
small residue substitutions for Pro101 do not alter the KM for phosphoenolpyruvate and shikimate 3-phosphate
-
additional information
additional information
-
kinetic parameters of native and diethyldicarbonate-inactivated enzyme
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000012
5-enolpyruvylshikimate 3-phosphate
-
5-enpolpyruvylshikimate 3-phosphate ketal formation by hydrolysis of radiolabelled 5-enpolpyruvylshikimate 3-phosphate, pH 7.0, 25°C
0.026
3-phosphoshikimate
50 mM KCl, mutant D313C, cosubstrate: phosphoenolpyruvate
0.3
3-phosphoshikimate
50 mM KCl, mutant K22A value above 0.3, cosubstrate: phosphoenolpyruvate
0.41
3-phosphoshikimate
50 mM KCl, mutant H385A, cosubstrate: phosphoenolpyruvate
1.1
3-phosphoshikimate
50 mM KCl, mutant D313L, cosubstrate: phosphoenolpyruvate
1.1
3-phosphoshikimate
50 mM KCl, mutant E341Q, cosubstrate: phosphoenolpyruvate
1.2
3-phosphoshikimate
50 mM KCl, mutant D313A, cosubstrate: phosphoenolpyruvate
1.7
3-phosphoshikimate
50 mM KCl, mutant E341M, cosubstrate: phosphoenolpyruvate
1.8
3-phosphoshikimate
50 mM KCl, mutant D313N, cosubstrate: phosphoenolpyruvate
3
3-phosphoshikimate
50 mM KCl, mutant K22R value above 0.3, cosubstrate: phosphoenolpyruvate
3.6
3-phosphoshikimate
50 mM KCl, mutant E341C, cosubstrate: phosphoenolpyruvate
4.2
3-phosphoshikimate
50 mM KCl, mutant E341A, cosubstrate: phosphoenolpyruvate
14
3-phosphoshikimate
wild-type AroA, 100 mM KCl, cosubstrate: phosphoenolpyruvate
32
3-phosphoshikimate
C-terminal His6-tagged AroA, 50 mM KCl, cosubstrate: phosphoenolpyruvate
100
3-phosphoshikimate
C-terminal His6-tagged AroA, 100 mM KCl, cosubstrate: phosphoenolpyruvate
0.026
phosphoenolpyruvate
50 mM KCl, mutant D313C, cosubstrate: 3-phosphoshikimate
0.3
phosphoenolpyruvate
50 mM KCl, mutant K22A value above 0.3, cosubstrate: 3-phosphoshikimate
0.41
phosphoenolpyruvate
50 mM KCl, mutant H385A, cosubstrate: 3-phosphoshikimate
1.1
phosphoenolpyruvate
50 mM KCl, mutant D313L, cosubstrate: 3-phosphoshikimate
1.1
phosphoenolpyruvate
50 mM KCl, mutant E341Q, cosubstrate: 3-phosphoshikimate
1.2
phosphoenolpyruvate
50 mM KCl, mutant D313A, cosubstrate: 3-phosphoshikimate
1.7
phosphoenolpyruvate
50 mM KCl, mutant E341M, cosubstrate: 3-phosphoshikimate
1.8
phosphoenolpyruvate
50 mM KCl, mutant D313N, cosubstrate: 3-phosphoshikimate
3
phosphoenolpyruvate
50 mM KCl, mutant K22R value above 0.3, cosubstrate: 3-phosphoshikimate
3.6
phosphoenolpyruvate
50 mM KCl, mutant E341C, cosubstrate: 3-phosphoshikimate
4.2
phosphoenolpyruvate
50 mM KCl, mutant E341A, cosubstrate: 3-phosphoshikimate
14
phosphoenolpyruvate
wild-type AroA, 100 mM KCl, cosubstrate: 3-phosphoshikimate
15
phosphoenolpyruvate
mutant A183T, in presence of 1 mM shikimate 3-phosphate
21
phosphoenolpyruvate
mutant G96A/A183T, in presence of 1 mM shikimate 3-phosphate
29.7
phosphoenolpyruvate
mutant G96A, in presence of 1 mM shikimate 3-phosphate
32
phosphoenolpyruvate
C-terminal His6-tagged AroA, 50 mM KCl, cosubstrate: 3-phosphoshikimate
100
phosphoenolpyruvate
C-terminal His6-tagged AroA, 100 mM KCl, cosubstrate: 3-phosphoshikimate
0.0000045
phosphoenolpyruvate
-
5-enpolpyruvylshikimate 3-phosphate ketal formation in presence of shikimate 3-phosphate and equimolar phosphoenolpyruvate
0.000049
phosphoenolpyruvate
-
5-enpolpyruvylshikimate 3-phosphate ketal formation in presence of shikimate 3-phosphate and 6.7 equivalents of phosphoenolpyruvate
0.00008
phosphoenolpyruvate
-
5-enpolpyruvylshikimate 3-phosphate ketal formation in presence of shikimate 3-phosphate and 6.7 equivalents of phosphoenolpyruvate and 10 mM phosphate
additional information
phosphoenolpyruvate
kcat/KM: 240000 1/M*s, mutant P101G
additional information
phosphoenolpyruvate
-
kcat/KM: 240000 1/M*s, mutant P101G
additional information
phosphoenolpyruvate
kcat/KM: 280000 1/M*s, mutant P101A
additional information
phosphoenolpyruvate
-
kcat/KM: 280000 1/M*s, mutant P101A
additional information
phosphoenolpyruvate
kcat/KM: 290000 1/M*s, mutant P101S
additional information
phosphoenolpyruvate
-
kcat/KM: 290000 1/M*s, mutant P101S
additional information
phosphoenolpyruvate
kcat/KM: 41000 1/M*s, mutant P101L
additional information
phosphoenolpyruvate
-
kcat/KM: 41000 1/M*s, mutant P101L
additional information
shikimate 3-phosphate
kcat/KM: 200000 1/M*s, mutant P101S
additional information
shikimate 3-phosphate
-
kcat/KM: 200000 1/M*s, mutant P101S
additional information
shikimate 3-phosphate
kcat/KM: 390000 1/M*s, mutant P101A
additional information
shikimate 3-phosphate
-
kcat/KM: 390000 1/M*s, mutant P101A
additional information
shikimate 3-phosphate
kcat/KM: 390000 1/M*s, mutant P101G
additional information
shikimate 3-phosphate
-
kcat/KM: 390000 1/M*s, mutant P101G
additional information
shikimate 3-phosphate
kcat/KM: 62000 1/M*s, mutant P101L
additional information
shikimate 3-phosphate
-
kcat/KM: 62000 1/M*s, mutant P101L
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000039
(3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
+/-0.6 nM
0.00076
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
+/-200 nM
0.000016
(3R,4S,5R)-5-((R)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid
versus 3-phosphoshikimate
0.00075
(3R,4S,5R)-5-((S)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid
versus 3-phosphoshikimate
0.0000078
(3R,4S,5R)-5-[(2R)-1,1-difluoro-3-hydroxy-3-oxo-2-phosphonooxy-propan-2-yl]oxy-4-hydroxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
+/-0.5 nM
0.0009
N-phosphonomethylglycine
-
vs. shikimate 3-phosphate, recombinant enzyme
additional information
glyphosate
any substitutions for residue Pro101 decrease glyphosate binding affinity and inhibitor potency
additional information
glyphosate
-
any substitutions for residue Pro101 decrease glyphosate binding affinity and inhibitor potency
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
glyphosate
Escherichia coli
more than 10 mM for mutant G96A/A183T
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18
62
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with inhibitor (3R,4S,5R)-5-((S)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid or with inhibitor (3R,4S,5R)-5-((R)-1-carboxy-1-phosphono-ethoxy)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid, 100 mg/ml recombinant enzyme in 2.5 M sodium formate with 10 mM inhibitor, hanging drop vapour diffusion method, 19°C, X-ray diffraction at -180°C using the rotation method on single flash-frozen crystals, structure determination and analysis at 1.5 and 1.9 A resolution, respectively
in presence of 10 mM inhibitor (3R,4S,5R)-5-[(2R)-1,1-difluoro-3-hydroxy-3-oxo-2-phosphonooxy-propan-2-yl]oxy-4-hydroxy-3-phosphonooxy-cyclohexene-1-carboxylic acid (2F-TI, PDB: 2PQ9), 2F-TI-binding induces large conformational change of Glu341 side chain compared to TI-binding, crystals: space group P2(1)2(1)2(1), unit cell parameters: a: 58.2, b: 85.1, c: 87.6, beta: 90°, hanging-drop vapour-diffusion, sodium format conditions, molecular replacement using PDB: 1G6S as model
mutants P101S and P101L in complex with shikimate 3-phosphate and with or without inhibitor glyphosate, long-range structural change in glyphosate binding site compared to wild-type, Gly96 and Thr97 are shifted towards the glyphosate-binding site, which gets slightly narrowed, crystals: space group: P2(1)2(1)2(1), unit cell parameters: a: 57.6-57.8, b: 85.1-85.6, c: 87.9-88.3, beta: 90°, hanging-drop vapour-diffusion, protein solution (37.5 mg/ml, 5 mM inhibitor and/or 5 mM shikimate 3-phosphate), 19°C, molecular replacement using PDB: 1G6S as model
purified recombinant wild-type and mutant enzymes in complex with the substrates, at 19°C, from 4 M sodium formate in presence of 5 mM 3-phosphoshikimate and 5 mM phosphoenolpyruvate, X-ray diffraction structure determination and analysis at 1.6 A resolution
semiempirical molecular modelling using, among others, the crystal structure of EPSPS mutant D313A (PDB: 1Q36) as model for assignment of protonation states of all basic amino acids in the active site: in the enzyme-tetrahedral reaction intermediate (TI) complex is residue His385 in a neutral form (with protonated epsilon-N atom) while residues Lys22, Lys340 and Lys411 are protonated, hydrogen bonds occur between Lys22 and the carboxylate oxygen atom of the phosphoenolpyruvate moiety of the TI, Asp313 has only minor effects on TI positioning within the active site but mediates as a base the attack of the TI C4-hydroxyl group on the TI methyl group prior to EPSP formation
using the hanging drop, vapor-diffusion method in the presence of 5 mM 3-phosphoshikimate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A183T
38fold decrease in phosphoenolpyruvate-binding affinity, more solvent-exposed tryptophan residues and lower stability against guanidine hydrochloride compared to wild-type and mutant G96A, midpoint guanidine hydrochloride concentration of unfolding: 0.7 M, higher structural flexibility and decrease of secondary structure (28% alpha helix, 35% beta sheet) compared to wild-type (40% alpha helix, 31% beta sheet) and lowest resistance against proteolysis, residue A183 located on the exterior in the N-terminal domain
D313A
D313C
compared to wild-type mutations of D313 causes kcat to decrease. In the mutant D313C the kcat is smaller than in other mutants (1200fold). Cys is ionizable and can potentially act as an acid/base catalyst, or the thiolate form can stabilize cationic intermediates electrostatically. This accounts for the higher catalytic activity for D313C than for D313A: The effects on Km(3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest
D313L
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
D313N
E341A
E341C
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
E341M
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
E341Q
G96A
G96A/A183T
glyphosate-insensitive, 8fold decrease in phosphoenolpyruvate-binding affinity, more solvent-exposed tryptophan residues and lower stability against guanidine hydrochloride compared to wild-type and mutant G96A, midpoint guanidine hydrochloride concentration of unfolding: 0.65 M, higher structural flexibility and decrease of secondary structure (36% alpha helix, 38% beta sheet) compared to wild-type (40% alpha helix, 31% beta sheet)
H385A
K22A
K22R
P101A
slight decrease in catalytic efficiency, decreased inhibitory potency of glyphosate
P101G
slight decrease in catalytic efficiency, decreased inhibitory potency of glyphosate
P101L
lowest catalytic efficiency, decreased inhibitory potency of glyphosate due to long-range conformational changes
P101S
T971I
the single site T97I mutation renders the enzyme sensitive to glyphosate and causes a substantial decrease in the affinity for phosphoenolpyruvate. Km (3-phosphoshikimate): 0.077 mM, Km (phosphoenolpyruvate): 0.38, kcat/Km (phosphoenolpyruvate): 23000/Msec, kcat/Km (3-phosphoshikimate): 1200000/Msec
T97I/P101S
mutant is essentially insensitive to glyphosate (Ki 2.4 mM) but maintains high affinity for the substrate phosphoenolpyruvate (Km: 0.1 mM) and 3-phosphoshikimate (Km: 0.077 mM). kcat/Km (phosphoenolpyruvate): 57000/Msec, kcat/Km (3-phosphoshikimate): 740000/Msec. The crystal structure at 1.7 A resolution reveals that the dual mutation causes a shift of residue Gly96 toward the glyphosate binding site, impairing efficient binding of glyphosate, while the side chain of Ile97 points away from the substrate binding site, facilitating phosphoenolpyruvate utilization
D242A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
D348A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
R100A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
T42M
-
site-directed mutagenesis, the mutation is responsible for the glyphosate resistance and the low Km for phosphoenolpyruvate
additional information
D313A
site-directed mutagenesis, comparison of the mutant active site and substrate binding structures to those of the wild-type enzyme
D313A
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
D313N
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
E341A
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
E341Q
compared to wild-type mutations of D313 causes kcat to decrease up to 30000fold while the effects on Km (3-phosphoshikimate) or Km (phosphoenolpyruvate) are modest, never more than 40fold
G96A
glyphosate-insensitive, 31fold decrease in phosphoenolpyruvate-binding affinity, little change with respect to structural flexibility and stability compared to wild-type, lower structural flexibility than wild-type and mutants A183T and G96A/A183T, midpoint guanidine hydrochloride concentration of unfolding: 1.1 M, residue Gly96 located at interphase between two domains
H385A
compared to wild-type mutation of H385 causes a 78fold decrease in kcat. Mutation has a 37fold effect on Km (phosphoenolpyruvate), almost no effect on Km (3-phosphoshikimate)
K22A
compared to wild-type, K22A mutation causes a more than760fold increase in Km (phosphoenolpyruvate) and a more than 100fold increase in Km(3-phosphoshikimate), indicating an important role in binding both substrates
K22R
compared to wild-type, K22R mutation has only a 10fold effect on kcat, presumably reflecting electrostatic stabilization of the anionic leaving groups in tetrahedral intermediate breakdown or possibly general acid catalysis by the guanidinium group. K22A mutation causes a 60fold increase in Km (phosphoenolpyruvate)
P101S
slight decrease in catalytic efficiency, decreased inhibitory potency of glyphosate due to long-range conformational changes, flexibility of Ser101 side chain disables hydrophobic bonding with carbonyl oxygen of Thr97
P101S
the substrate binding affinities, as reflected by the respective Km values, are only slightly decreased for the P101S mutant. Km (3-phosphoshikimate): 0.071 mM, Km (phosphoenolpyruvate): 0.071, kcat/Km (phosphoenolpyruvate): 230000/Msec, kcat/Km (3-phosphoshikimate): 240000/Msec. Mutant P101S is moderately inhibited by glyphosate
additional information
-
construction of chimeric mutants by fusing the N-terminal part of the Escherichia coli enzyme with the C-terminal part of the enzyme from Salmonella typhimurium, the chimeric mutant shows a 6fold lower Km for phosphoenolpyruvate, a 5fold higher Ki for glyphosate, and a 9fold higher specific activity than the wild-type enzyme from Escherichia coli
additional information
-
construction of chimeric mutants by fusing the N-terminal part of the Escherichia coli enzyme with the C-terminal part of the enzyme from Salmonella typhimurium, the chimeric mutant shows a 6fold lower Km for phosphoenolpyruvate, a 5fold higher Ki for glyphosate, and a 9fold higher specific activity than the wild-type enzyme from Escherichia coli, construction of glyphosate-resistant transgenic Nicotiana tabacum plants expressing the chimeric mutant aroA-M1 using the Agrobacterium tumefaciens strain LBA 4404 infection system
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete unfolding of the protein at 2.5 M guanidine hydrochloride at pH 7.8 (midpoint guanidine hydrochloride concentration of unfolding: 0.8 +/-0.1 M), enhanced flexibility, lower stability and increased proteolysis of mutants A183T and G96A/A183T compared to wild-type and mutant G96A as revealed by susceptibility to proteolytic digestion with trypsin, thermolysin, pronase (25°C for various time intervals), unfolding profiles (intrinsic tryptophan fluorescence measurements at 340 nm) after treatment with guanidine hydrochloride (30 min at 25°C) and dynamic quenching with acrylamide or not, and secondary structure determination by circular dichroism spectroscopy
dithiothreitol reverses aggregation which sometimes occurs after storage at -20°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.5, 50 mM KCl, 0.4 mM dithiothreitol, 50% v/v glycerol, at least 4 months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from supernatant from 25% (w/v) ammonium sulfate precipitation of crude bacterial extracts, Q-sepharose anion exchange chromatography (NaCl gradient elution) and FPLC (Mono-Q column, NaCl gradient elution)
recombinant enzyme, ammonium sulfate, DEAE-Sephacel, phenyl-Sepharose, phosphocellulose chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant G96A is expressed in Escherichia coli BL21 cells and Oryza sativa
overexpression of wild-type, His-tagged wild-type and several mutant enzymes in Escherichia coli
wild-type and mutants in pET-24d for expression in Escherichia coli BL21(DE3)
expression of the wild-type enzyme and of the chimeric mutant aroA-M1, comprising N-terminal part of the Escherichia coli enzyme and the C-terminal part of the enzyme from Salmonella typhimurium in strain XL1-Blue
-
expression of the wild-type enzyme, of the chimeric mutant aroA-M1, comprising N-terminal part of the Escherichia coli enzyme and the C-terminal part of the enzyme from Salmonella typhimurium, and of T42M-aroA mutant in strain BL21(DE3)
-
expression of wild-type and chimeras of Salmonella and Escherichia coli mutant enzymes in Escherichia coli
-
mutant enzyme G96A/A183T is transferred to Brassica napus via Agrobacterium-mediated transformation. Transgenic plants are resistant to glyphosate at a concentration of 10 mM whereas the non-transformed control plants are unable to survive 1 mM glyphosate
-
subcloned from bacteriophage lambdapserC into multicopy plasmid pAT153 with subsequent transformation of Escherichia coli AB2829 CGSC2829 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
differential inhibition of class I and class II EPSPS by tetrahedral reaction intermediate-analogues possibly due to alteration of open-close transition during catalysis and/or upon inhibitor binding but not due to energy differences during complex formation
synthesis
drug development
-
protonated enolpyruvylshikimate 3-phosphate (cation) intermediate as potential target for inhibitor design
synthesis
enzyme is a target for development and synthesis of antimicrobial drugs
synthesis
-
enzyme is a target for development and synthesis of antimicrobial drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coggins, J.R.; Duncan, K.; Anton, I.A.; Boocock, M.R.; Chaudhuri, S.; Lambert, J.M.; Lewendon, A.; Millar, G.; Mousdale, D.M.; Smith, D.D.S.
The anatomy of a multifunctional enzyme
Biochem. Soc. Trans.
15
754-759
1987
Aspergillus nidulans, Saccharomyces cerevisiae, Escherichia coli, Neurospora crassa, Salmonella enterica subsp. enterica serovar Typhimurium
Lewendon, A.; Coggins, J.R.
3-Phosphoshikimate 1-carboxyvinyltransferase from Escherichia coli
Methods Enzymol.
142
342-348
1987
Escherichia coli, Klebsiella pneumoniae, Neurospora crassa, Pisum sativum, Salmonella enterica subsp. enterica serovar Typhimurium
Lewendon, A.; Coggins, J.R.
Purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli
Biochem. J.
213
187-191
1983
Escherichia coli
Duncan, K.; Lewendon, A.; Coggins, J.R.
The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain of Escherichia coli
FEBS Lett.
165
121-127
1984
Escherichia coli
Gruys, K.J.; Walker, M.C.; Sikorski, J.A.
Substrate synergism and the steady-state kinetic reaction mechanism for EPSP synthase from Escherichia coli
Biochemistry
31
5534-5544
1992
Escherichia coli
Huynh, Q.K.
Reaction of 5-enol-pyruvoylshikimate-3-phosphate synthase with diethyl pyrocarbonate: evidence for an essential histidine residue
Arch. Biochem. Biophys.
258
233-239
1987
Escherichia coli
Huynh, Q.K.
Inactivation of 5-enolpyruvylshikimate 3-phosphate synthase by its substrate analogue pyruvate in the presence of sodium cyanoborohydride
Biochem. Biophys. Res. Commun.
185
317-322
1992
Escherichia coli
Huynh, Q.K.
5-Enolpyruvylshikimate-3-phosphate synthase from Escherichia coli--the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411
Arch. Biochem. Biophys.
284
407-412
1991
Escherichia coli, Escherichia coli N5259
Abdel-Meguid, S.S.; Smith, W.W.; Bild, G.S.
Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli
J. Mol. Biol.
186
673
1985
Escherichia coli
Shuttleworth, W.A.; Evans, J.N.S.
The H385N mutant of 5-enolpyruvylshikimate-3-phosphate synthase: kinetics, fluorescence, and nuclear magnetic resonance studies
Arch. Biochem. Biophys.
334
37-42
1996
Escherichia coli
Jakeman, D.L.; Mitchell, D.J.; Shuttleworth, W.A.; Evans, J.N.
On the mechanism of 5-enolpyruvylshikimate-3-phosphate synthase
Biochemistry
37
12012-12019
1998
Escherichia coli
He, M.; Yang, Z.Y.; Nie, Y.F.; Wang, J.; Xu, P.
A new type of class I bacterial 5-enopyruvylshikimate-3-phosphate synthase mutants with enhanced tolerance to glyphosate
Biochim. Biophys. Acta
1568
1-6
2001
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Stauffer, M.E.; Young, J.K.; Evans, J.N.S.
Shikimate-3-phosphate binds to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase
Biochemistry
40
3951-3957
2001
Escherichia coli (P0A6D3)
Schonbrunn, E.; Eschenburg, S.; Shuttleworth, W.A.; Schloss, J.V.; Amrhein, N.; Evans, J.N.S.; Kabsch, W.
Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail
Proc. Natl. Acad. Sci. USA
98
1376-1380
2001
Escherichia coli (P0A6D3)
Eschenburg, S.; Healy, M.L.; Priestman, M.A.; Lushington, G.H.; Schonbrunn, E.
How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli
Planta
216
129-135
2002
Escherichia coli, Klebsiella pneumoniae
Mizyed, S.; Wright, J.E.; Byczynski, B.; Berti, P.J.
Identification of the catalytic residues of AroA (Enolpyruvylshikimate 3-phosphate synthase) using partitioning analysis
Biochemistry
42
6986-6995
2003
Escherichia coli (P0A6D3)
Priestman, M.A.; Healy, M.L.; Becker, A.; Alberg, D.G.; Bartlett, P.A.; Lushington, G.H.; Schonbrunn, E.
Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail
Biochemistry
44
3241-3248
2005
Escherichia coli (P0A6D3), Escherichia coli
He, M.; Nie, Y.F.; Xu, P.
A T42M substitution in bacterial 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) generates enzymes with increased resistance to glyphosate
Biosci. Biotechnol. Biochem.
67
1405-1409
2003
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Eschenburg, S.; Kabsch, W.; Healy, M.L.; Schonbrunn, E.
A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states
J. Biol. Chem.
278
49215-49222
2003
Escherichia coli (P0A6D3), Escherichia coli
Wang, H.Y.; Li, Y.F.; Xie, L.X.; Xu, P.
Expression of a bacterial aroA mutant, aroA-M1, encoding 5-enolpyruvylshikimate-3-phosphate synthase for the production of glyphosate-resistant tobacco plants
J. Plant Res.
116
455-460
2003
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Clark, M.E.; Berti, P.J.
Enolpyruvyl activation by enolpyruvylshikimate-3-phosphate synthase
Biochemistry
46
1933-1940
2007
Escherichia coli
Priestman, M.A.; Healy, M.L.; Funke, T.; Becker, A.; Schoenbrunn, E.
Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate
FEBS Lett.
579
5773-5780
2005
Escherichia coli (P0A6D3), Escherichia coli
Kahrizi, D.; Salmanian, A.H.; Afshari, A.; Moieni, A.; Mousavi, A.
Simultaneous substitution of Gly96 to Ala and Ala183 to Thr in 5-enolpyruvylshikimate-3-phosphate synthase gene of E. coli (k12) and transformation of rapeseed (Brassica napus L.) in order to make tolerance to glyphosate
Plant Cell Rep.
26
95-104
2007
Escherichia coli
Funke, T.; Healy-Fried, M.L.; Han, H.; Alberg, D.G.; Bartlett, P.A.; Schoenbrunn, E.
Differential inhibition of class I and class II 5-enolpyruvylshikimate 3-phosphate synthases by tetrahedral reaction intermediate analogues
Biochemistry
46
13344-13351
2007
Staphylococcus aureus, Escherichia coli (P0A6D3), Escherichia coli, Agrobacterium sp. (Q9R4E4), Agrobacterium sp., Agrobacterium sp. CP4 (Q9R4E4)
Haghani, K.; Salmanian, A.H.; Ranjbar, B.; Zakikhan-Alang, K.; Khajeh, K.
Comparative studies of wild type Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase with three glyphosate-insensitive mutated forms: activity, stability and structural characterization
Biochim. Biophys. Acta
1784
1167-1175
2008
Escherichia coli (P0A6D3), Escherichia coli
de Souza, A.X.; SantAnna, C.M.
5-Enolpyruvylshikimate-3-phosphate synthase: determination of the protonation state of active site residues by the semiempirical method
Bioorg. Chem.
36
113-120
2008
Escherichia coli (P0A6D3)
Healy-Fried, M.L.; Funke, T.; Priestman, M.A.; Han, H.; Schoenbrunn, E.
Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase
J. Biol. Chem.
282
32949-32955
2007
Escherichia coli (P0A6D3), Escherichia coli
Berti, P.J.; Chindemi, P.
Catalytic residues and an electrostatic sandwich that promote enolpyruvyl shikimate 3-phosphate synthase (AroA) catalysis
Biochemistry
48
3699-3707
2009
Escherichia coli (P0A6D3)
Funke, T.; Yang, Y.; Han, H.; Healy-Fried, M.; Olesen, S.; Becker, A.; Schoenbrunn, E.
Structural basis of glyphosate resistance resulting from the double mutation Thr97 Ile and Pro101 Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli
J. Biol. Chem.
284
9854-9860
2009
Escherichia coli (P0A6D3), Escherichia coli
Nasr Ramzi, S.; Sohani, M.; Shirzadian-Khorramabad, R.; Asghari, J.; Amininasab, M.
Enhancement of glyphosate tolerance in rice (Oryza sativa L.) through mutation induction in EPSPS (5-enolpyruvylshikimate-3-phosphate synthase)
Plant Gene
22
100225
2020
Escherichia coli (P0A6D3)
-
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