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Information on EC 2.5.1.19 - 3-phosphoshikimate 1-carboxyvinyltransferase
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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
-
interneurons
- glyphosate
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firing
-
hyperpolarization
-
electrophysiological
-
antidromic
-
summation
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subthreshold
- bicuculline
-
gabaa
-
disynaptic
-
non-nmda
-
tetanic
-
6-cyano-7-nitroquinoxaline-2,3-dione
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volley
-
schaffer
-
quantal
-
unitary
-
paired-pulse
-
orthodromic
-
glyphosate-resistant
-
short-latency
-
thalamocortical
- biotechnology
-
electrotonic
-
reticulospinal
- radiatum
-
homonymous
- drug development
- agriculture
- synthesis
-
interstimulus
-
funiculus
-
suprathreshold
-
preganglionic
-
low-threshold
-
impale
-
decerebrate
- biocytin
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afterhyperpolarization
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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-enolpyruvylshikimate 5-phosphate synthase
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-
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3-enolpyruvylshikimic acid-5-phosphate synthetase
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3-phosphoshikimate 1-carboxyvinyl-transferase
3-phosphoshikimate-1-carboxyvinyl-transferase
5'-enolpyruvylshikimate-3-phosphate synthase
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-
-
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5-enol-pyruvyl-shikimate-3-phosphate synthase
5-enol-pyruvylshikimate 3-phosphate synthase
5-enol-pyruvylshikimate-3-phosphate synthase
5-enolpyruvyl-3-phosphoshikimate synthase
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-
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5-enolpyruvylshikimate 3-phosphate synthase
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-enolpyruvylshikimate-3phosphate synthase
5-enolpyruvylshikimic acid-3-phosphate synthase
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-
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5-enopyruvylshikimate-3-phosphate synthase
5-enoylpyruvylshikimate 3-phosphate synthase
A1501 EPSPS
AroA
AroA(1398)
AroA(A1501)
AroA1398
DsaroA
Dunaliella salina 5-enolpyruvylshikimate-3-phosphate synthase
Dunaliella salina EPSP synthase
enolpyruvylshikimate phosphate synthase
enolpyruvylshikimate-3-phosphate synthase
EPSP synhthase
EPSP synthase
EPSPS
G2 5-enolpyruvyl shikimate 3-phosphate synthase
G2 EPSPS
Mt EPSPS
Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase
synthase, 5-enolpyruvoylshikimate 3-phosphate
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-
-
-
additional information
5-enol-pyruvyl-shikimate-3-phosphate synthase
Limnospira fusiformis Hegewald 1976/83
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-
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5-enolpyruvylshikimate 3-phosphate synthase
class II, glyphosate-tolerant
5-enolpyruvylshikimate 3-phosphate synthase
class II, glyphosate-tolerant
-
5-enolpyruvylshikimate 3-phosphate synthase
class I, glyphosate-sensitive
5-enolpyruvylshikimate 3-phosphate synthase
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class II, glyphosate-tolerant
5-enolpyruvylshikimate-3-phosphate synthase
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-
-
-
5-enolpyruvylshikimate-3-phosphate synthase
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5-enolpyruvylshikimate-3-phosphate synthase
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-
5-enolpyruvylshikimate-3phosphate synthase
Bacteria ATX1398
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-
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AroA(1398)
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glyphosate-tolerant gene product from strain ATX1398 that lacks protein sequence hallmarks of class II EPSP synthases
AroA(1398)
Bacteria ATX1398
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glyphosate-tolerant gene product from strain ATX1398 that lacks protein sequence hallmarks of class II EPSP synthases
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AroA1398
Bacteria ATX1398
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-
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enolpyruvylshikimate phosphate synthase
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-
-
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enolpyruvylshikimate phosphate synthase
Bacteria ATX1398
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-
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EPSP synthase
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-
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EPSP synthase
Bacteria ATX1398
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-
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EPSP synthase
Limnospira fusiformis Hegewald 1976/83
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-
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G2 5-enolpyruvyl shikimate 3-phosphate synthase
glyphosate resistant
G2 5-enolpyruvyl shikimate 3-phosphate synthase
glyphosate resistant
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Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase
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Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase
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-
additional information
enzyme belongs to the family of enolpyruvyl transferases
additional information
-
class II 5-enolpyruvylshikimate-3-phosphate synthases are less sensitive to glyphosate in contrary to class I 5-enolpyruvylshikimate-3-phosphate synthases which are highly sensitive to inhibition with glyphosate
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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
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-
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phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
proposed mechanism
-
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
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
-
phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
ordered substrate binding with 3-phosphoshikimate being bound first
-
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
enolpyruvate group transfer
enolpyruvate group transfer
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-
-
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enolpyruvate group transfer
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induced-fit mechanism, formation of a 2-(S) configured tetrahedral reaction intermediate by covalent linkage of the two substrates
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
induced-fit mechanism, formation of a 2-(S) configured tetrahedral reaction intermediate by covalent linkage of the two substrates
enolpyruvate group transfer
-
induced-fit mechanism, formation of a 2-(S) configured tetrahedral reaction intermediate by covalent linkage of the two substrates
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
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
-
-
?
phosphate + 5-enolpyruvylshikimate 3-phosphate
shikimate 3-phosphate + phosphoenolpyruvate
-
reverse reaction
phosphoenolpyruvate generation coupled to pyruvate kinase and lactate dehydrogenase and monitored spectrophotometrically at 340 nm, pH7.0, in presence of ADP, NADH, MgCl2
-
r
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
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in aromatic acid biosynthesis
-
-
?
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
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
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
-
involved in aromatic acid biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
critical enzyme in the shikimate pathway
-
-
?
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
sixth enzyme in the shikimate pathway. The enzyme is widely involved in glyphosate tolerant transgenic plants because it is the primary target of the nonselective herbicide lyphosate
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
sixth enzyme in the shikimate pathway. The enzyme is widely involved in glyphosate tolerant transgenic plants because it is the primary target of the nonselective herbicide lyphosate
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-
?
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
-
-
-
r
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-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
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
-
-
?
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
-
-
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
-
part of shikimate pathway
-
-
?
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
-
-
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
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
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
-
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
-
part of shikimate pathway
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
-
-
-
?
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
-
part of shikimate pathway
-
-
?
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
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
-
?
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
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
-
?
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
-
key 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
-
-
?
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
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Limnospira fusiformis Hegewald 1976/83
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Lyngbya sp.
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
the 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
phosphate induces conformational change on the MtEPSPS structure
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
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
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
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
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
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
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Tolypothrix sp.
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
pH 7, start with phosphoenolpyruvate, with or without inhibitor glyphosate
fluorescence-based coupled enzymatic assay including xanthine oxidase, purine nucleoside phosphorylase, inosine, horseradish peroxidase and Amplex Red
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
shikimate 3-phosphate binding site primarily at the N-terminal domain of the enzyme, phosphoenolpyruvate-binding mainly a the C-terminal domain
-
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
Bacteria ATX1398
-
pH 7, start with phosphoenolpyruvate, with or without inhibitor glyphosate
fluorescence-based coupled enzymatic assay including xanthine oxidase, purine nucleoside phosphorylase, inosine, horseradish peroxidase and Amplex Red
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
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
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
plant
-
pH 7, start with phosphoenolpyruvate, with or without inhibitor glyphosate
fluorescence-based coupled enzymatic assay including xanthine oxidase, purine nucleoside phosphorylase, inosine, horseradish peroxidase and Amplex Red
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
forward reaction
phosphate generation monitored by native gel analyses and subsequent calciumphosphate precipitation upon soaking in substrate solution in presence or absence of inhibitor glyphosate
-
r
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
1 mM shikimate 3-phosphate and 0.05-1.0 mM phosphoenolpyruvate
detection of inorganic phosphate generation by Malachite Green dye assay according to Lanzetta
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
1 mM shikimate 3-phosphate and 0.05-1.0 mM phosphoenolpyruvate
detection of inorganic phosphate generation by Malachite Green dye assay according to Lanzetta
-
?
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
-
?
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
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
activity independent of transit peptide (N-terminal 70 residues)
growth of transformed Escherichia coli lacking endogenous EPSP synthase on M9 minimal medium by sustaining synthesis of aromatic amino acids through introduced 5-enolpyruvylshikimate 3-phosphate synthesis, leading to 10fold increase in glyphosate tolerance in bacteria compared to controls
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
activity independent of transit peptide (N-terminal 70 residues)
growth of transformed Escherichia coli lacking endogenous EPSP synthase on M9 minimal medium by sustaining synthesis of aromatic amino acids through introduced 5-enolpyruvylshikimate 3-phosphate synthesis, leading to 10fold increase in glyphosate tolerance in bacteria compared to controls
-
?
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
-
?
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
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
malachite green dye assay, 28°C
-
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
malachite green dye assay, 28°C
-
-
?
shikimate 3-phosphate + phosphoenolpyruvate
phosphate + 5-enpolpyruvylshikimate 3-phosphate
-
via formation of a 2-(S)-tetrahedral reaction intermediate (TI), pH 7.5, 25°C, 20 min
examination by malachite green phosphate-release assay
-
?
additional information
?
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
additional information
?
-
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
additional information
?
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-O-(1-carboxyvinyl)-3-phosphoshikimate
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in aromatic acid biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
involved in aromatic acid biosynthesis
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
critical enzyme in the shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
sixth enzyme in the shikimate pathway. The enzyme is widely involved in glyphosate tolerant transgenic plants because it is the primary target of the nonselective herbicide lyphosate
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
sixth enzyme in the shikimate pathway. The enzyme is widely involved in glyphosate tolerant transgenic plants because it is the primary target of the nonselective herbicide lyphosate
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
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-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-enolpyruvylshikimate 3-phosphate
-
part of shikimate pathway
-
-
?
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
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
-
?
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
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
key 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
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Limnospira fusiformis Hegewald 1976/83
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Lyngbya sp.
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
the 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
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
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
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
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
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
-
-
-
-
r
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
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
Tolypothrix sp.
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
r
phosphoenolpyruvate + 3-phosphoshikimate
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate
-
-
-
-
?
additional information
?
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
additional information
?
-
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
additional information
?
-
sixth enzyme in shikimate pathway, biosynthesis of aromatic amino acids
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Na+
NH4+
Rb+
strong activation of forward reaction, effectiveness of activation in descending order: NH4Cl, Rb+, K+
additional information
K+
strong activation of forward reaction, effectiveness of activation in descending order: NH4Cl, Rb+, K+
additional information
-
not activated by Ba2+, Ca2+, Mg2+, Ni2+ or Sr2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
(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
(Z)-3-fluorophosphoenolpyruvate
-
competitive vs. phosphoenolpyruvate at saturated shikimate 3-phosphate concentration and vice versa
diethyldicarbonate
-
inactivation with a second-order rate constant of 220/M/min, subtstrates protect from inactivation, enzyme activity is recovered by treatment with hydroxylamine
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
shikimate 3-phosphate-5-carboxymethyl-(2R)-phosphonate
-
competitive vs. 5-enolpyruvylshikimate-3-phosphate and phosphate
shikimate 3-phosphate-5-carboxymethyl-(2S)-phosphonate
-
competitive vs. 5-enolpyruvylshikimate-3-phosphate and phosphate
(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, competitive inhibitor of EPSPS forward reaction, 460fold decrease in potency compared to glyphosate-sensitive class I EPSPS from Escherichia coli
(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-[(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, competitive inhibitor of EPSPS forward reaction, 120-fold decrease in potency compared to glyphosate-sensitive class I EPSPS from Escherichia coli
(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, non-potent competitive inhibitor of EPSPS forward reaction
(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)-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, competitive inhibitor of EPSPS forward reaction
(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, competitive inhibitor of EPSPS forward reaction, 8fold decrease in potency compared to glyphosate-sensitive class I EPSPS from Escherichia coli
(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
(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, competitive inhibitor of EPSPS forward reaction, 4-fold decrease in potency compared to glyphosate-sensitive class I EPSPS from Escherichia coli
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
glyphosate
-
competitor with phosphoenolpyruvate binding site, AroA(1398) transformation allows Escherichia coli DH5alpha and XL1 Blue colonies to grow on up to 200 mM glyphosate (non-transformed bacteria stop growing on 5 mM inhibitor), AroA(1398) integrated maize transgenic plant lines showed 54% survival upon glyphosate treatment compared to none of control plants
glyphosate
-
competitive inhibition of the wild-type enzyme, mutant T42M is less sensitive
glyphosate
Kd: 350 micromolar (pH 6.9, 25°C), binding induces conformational change that leads to increase in alpha helix (40% to 57%) and decrease in beta-sheet (30% to 23%) content (revealed by circular dichroism spectroscopy) and prevents access of solvent to core molecule (revealed by hydrogen/deuterium exchange, peptic digestion and LC-ESI-MS)
glyphosate
plant
-
plants do not survive glyphosate spray treatment (1.78 l/ha of a 480 g AE/L formulation) in the field
glyphosate
-
inhibits forward reaction only slightly at 0.2 mM but substantially at 20 mM
glyphosate
-
at 300 mM: no growth of Escherichia coli transformed with either EPSPS wild-type or mutant N130S
glyphosate
-
competitive inhibition of the wild-type enzyme, mutant T42M is less sensitive
glyphosate
-
slight inhibition, insensitivity is independent from cations, mechanism
N-phosphonomethylglycine
-
0.25 mM, 50% inhibition of NH4Cl activated enzyme, 75 mM, 50% inhibition of nonactivated enzyme
N-phosphonomethylglycine
-
0.006 mM, 50% inhibition of glyphosate-sensitve strain, 0.03 mM, 50% inhibition of glyphosate-resistant strain
N-phosphonomethylglycine
-
inhibition of enolpyruvate transfer, competitive vs. phosphoenolpyruvate
N-phosphonomethylglycine
-
competitive vs. phosphoenolpyruvate, noncompetitive vs. shikimate 3-phosphate, 5-enolpyruvylshikimate 3-phosphate and phosphate, not inhibited by non-herbicidal analogues of glyphosate, e.g. aminomethylphosphonic acid, glyphosine, i.e. bis-N-(phosphonomethyl)glycine, or iminodiacetic acid; pH-dependent
N-phosphonomethylglycine
-
0.0183 mM, 50% inhibition, 0.5 mM 96% inhibition, competitive vs. phosphoenolpyruvate, uncompetitive vs. shikimate 3-phosphate at pH 7.0, mechanism; pH-dependent
N-phosphonomethylglycine
-
noncompetitive vs. phosphate, competitive vs. phosphoenolpyruvate, uncompetitive vs. shikimate 3-phosphate
N-phosphonomethylglycine
-
-
N-phosphonomethylglycine
-
3 mM, 50% inhibition, 25 mM, 90% inhibition; trivial name glyphosate, non-selective herbicide "Round up", free acid or monoisopropylamine salt
N-phosphonomethylglycine
-
0.006-0.008 mM, 50% inhibition, 1 mM, complete inhibition
additional information
insensitive to inhibition by glyphosate exhibiting Ki and IC50 values of 1.2 and 5.2 mM, respectively; not inhibited by EDTA
-
additional information
-
insensitive to inhibition by glyphosate exhibiting Ki and IC50 values of 1.2 and 5.2 mM, respectively; not inhibited by EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4Cl
strong activation of forward reaction, effectiveness of activation in descending order: NH4Cl, Rb+, K+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
3-phosphoshikimate 1-carboxyvinyltransferase deficiency
Bacterial expression and isolation of Petunia hybrida 5-enol-pyruvylshikimate-3-phosphate synthase.
Amyotrophic Lateral Sclerosis
Abnormal EPSPs evoked by magnetic brain stimulation in hand muscle motoneurons of patients with amyotrophic lateral sclerosis.
Amyotrophic Lateral Sclerosis
Comparison of corticomotoneuronal EPSPs and macro-MUPs in amyotrophic lateral sclerosis.
Amyotrophic Lateral Sclerosis
Reduced corticomotoneuronal excitatory postsynaptic potentials (EPSPs) with normal Ia afferent EPSPs in amyotrophic lateral sclerosis.
Anaphylaxis
The 5-enolpyruvylshikimate-3-phosphate synthase of glyphosate-tolerant soybean expressed in Escherichia coli shows no severe allergenicity.
Colitis
Cyclooxygenase-2 contributes to dysmotility and enhanced excitability of myenteric AH neurones in the inflamed guinea pig distal colon.
Colitis
Synaptic facilitation and enhanced neuronal excitability in the submucosal plexus during experimental colitis in guinea-pig.
Diabetes Mellitus, Experimental
[Mechanisms of inhibition of synaptic transmission in the sympathetic ganglia of rats with alloxan diabetes]
Epilepsy
Spontaneous and stimulation-induced synchronized burst afterdischarges in the isolated CA1 of kainate-treated rats.
Herpes Zoster
Feedforward inhibitory control of sensory information in higher-order thalamic nuclei.
Hyperalgesia
In vivo patch-clamp analysis of response properties of rat primary somatosensory cortical neurons responding to noxious stimulation of the facial skin.
Hyperglycemia
Synapses on sympathetic neurons and parasympathetic neurons differ in their vulnerability to diabetes.
Hypersensitivity
Point mutation of a conserved arginine (104) to lysine introduces hypersensitivity to inhibition by glyphosate in the 5-enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis.
Infections
Amino Acid Biosynthetic Pathways Are Required for Klebsiella pneumoniae Growth in Immunocompromised Lungs and Are Druggable Targets during Infection.
Infections
Chronic lentiviral expression of inwardly rectifying K(+) channels (Kir2.1) reduces neuronal activity and downregulates voltage-gated potassium currents in hippocampus.
Infections
Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.
Infections
Delivery of herpes simplex virus amplicon-based vectors to the dentate gyrus does not alter hippocampal synaptic transmission in vivo.
Infertility, Male
Endogenous tassel-specific small RNAs-mediated RNA interference enables a novel glyphosate-inducible male sterility system for commercial production of hybrid seed in Zea mays L.
Meningitis
Progress in cloning, expression and purification of 5-enolpyruvylshikimate-3-phosphate synthase from pathogens causing meningitis.
Motor Neuron Disease
Spinal motoneuron function in lower motor neuron disease: normal corticomotoneuronal and peripheral Ia EPSPs in patients with spinal muscular atrophy.
Muscle Spasticity
Prolonged time course of population excitatory postsynaptic potentials in motoneurons of chronic stroke survivors.
Muscular Atrophy, Spinal
Spinal motoneuron function in lower motor neuron disease: normal corticomotoneuronal and peripheral Ia EPSPs in patients with spinal muscular atrophy.
Neoplasms
The 5-enolpyruvylshikimate-3-phosphate synthase of glyphosate-tolerant soybean expressed in Escherichia coli shows no severe allergenicity.
Neuralgia
Altered synaptic transmission in rat anterior cingulate cortex following peripheral nerve injury.
Porcine Reproductive and Respiratory Syndrome
Counting on inhibition and rate-dependent excitation in the auditory system.
Seizures
17beta-estradiol enhances NMDA receptor-mediated EPSPs and long-term potentiation.
Seizures
Epileptogenesis reduces the sensitivity of presynaptic gamma-aminobutyric acidB receptors on glutamatergic afferents in the amygdala.
Seizures
Mechanism of electrographic seizure generation in the hippocampal slice in Mg2+-free medium: the role of GABAa inhibition.
Seizures
Rapid chain generation of interpostsynaptic functional LINKs can trigger seizure generation: Evidence for potential interconnections from pathology to behavior.
Seizures
Recurrent excitatory connectivity in the dentate gyrus of kindled and kainic acid-treated rats.
Spasm
Adrenergic receptors modulate motoneuron excitability, sensory synaptic transmission and muscle spasms after chronic spinal cord injury.
Spasm
Changes in sensory-evoked synaptic activation of motoneurons after spinal cord injury in man.
Spasm
Polysynaptic excitatory postsynaptic potentials that trigger spasms after spinal cord injury in rats are inhibited by 5-HT1B and 5-HT1F receptors.
Spinal Cord Injuries
Adrenergic receptors modulate motoneuron excitability, sensory synaptic transmission and muscle spasms after chronic spinal cord injury.
Spinal Cord Injuries
Selectivity in synaptic changes caudal to acute spinal cord transection.
Stroke
Estimating the Time Course of Population Excitatory Postsynaptic Potentials in Motoneurons of Spastic Stroke Survivors.
Stroke
Prolonged time course of population excitatory postsynaptic potentials in motoneurons of chronic stroke survivors.
Syndactyly
Synaptic mechanisms of cortical representational plasticity: somatosensory and corticocortical EPSPs in reorganized raccoon SI cortex.
Tetanus
Cholinergic activity enhances hippocampal long-term potentiation in CA1 during walking in rats.
Tetanus
Long-term potentiation and depression in layer III and V pyramidal neurons of the cat sensorimotor cortex in vitro.
Tetanus
Long-term potentiation and N-methyl-D-aspartate receptors in the visual cortex of young rats.
Tetanus
Potentiation of excitatory postsynaptic potentials during and after repetitive stimulation in thin hippocampal sections.
Tetanus
Prenatal morphine exposure enhances seizure susceptibility but suppresses long-term potentiation in the limbic system of adult male rats.
Tetanus
Selective modulation of Ca(2+) influx pathways by 5-HT regulates synaptic long-term plasticity in the hippocampus.
Tetanus
Variance analysis of excitatory postsynaptic potentials in cat spinal motoneurons during posttetanic potentiation.
Tuberculosis
Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis.
Tuberculosis
Dynamics of glyphosate-induced conformational changes of Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.19) determined by hydrogen-deuterium exchange and electrospray mass spectrometry.
Tuberculosis
One-step purification of 5-enolpyruvylshikimate-3-phosphate synthase enzyme from Mycobacterium tuberculosis.
Tuberculosis
Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis.
Tuberculosis
Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis.
Whooping Cough
Comparison of the actions of adenosine at pre- and postsynaptic receptors in the rat hippocampus in vitro.
Whooping Cough
Comparison of the actions of baclofen at pre- and postsynaptic receptors in the rat hippocampus in vitro.
Whooping Cough
Distinct muscarinic receptor subtypes suppress excitatory and inhibitory synaptic responses in cortical neurons.
Whooping Cough
Presynaptic inhibition of excitatory synaptic transmission mediated by alpha adrenergic receptors in area CA3 of the rat hippocampus in vitro.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
3-phosphoshikimate
-
pH 7.0, recombinant enzyme, in presence of 100 mM KCl
0.0019
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, mutant enzyme G99A
0.00195
5-enolpyruvylshikimate 3-phosphate
reverse reaction, in the presence of 50 mM KCl
0.002
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, wild-type enzyme
0.0025
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, mutant enzyme L104P
0.003
5-enolpyruvylshikimate 3-phosphate
-
recombinant overproducing strain
0.343
phosphate
reverse reaction, in the presence of 50 mM KCl
0.0018
phosphoenolpyruvate
-
pH 7.0, 30°C, mutant StaroA-T42M
0.011
phosphoenolpyruvate
-
wild type enzyme, at 28°C, pH not specified in the publication
0.023
phosphoenolpyruvate
in the presence of 1 mM NH4Cl and 100 mM KCl
0.032
phosphoenolpyruvate
-
mutant enzyme A187T, at 28°C, pH not specified in the publication
0.0436
phosphoenolpyruvate
-
pH 7.0, 30°C, wild-type StaroA
0.049
phosphoenolpyruvate
-
mutant enzyme T101A/A187T, at 28°C, pH not specified in the publication
0.055
phosphoenolpyruvate
-
+/-0.0014 mM, mutant N130S in bacterial extact
0.081
phosphoenolpyruvate
-
mutant enzyme T101A, at 28°C, pH not specified in the publication
0.085
phosphoenolpyruvate
in the presence of 1 mM NH4Cl and 10 mM KCl
0.0952
phosphoenolpyruvate
+/-0.00573 mM, full-length G2 EPSPS, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
0.0968
phosphoenolpyruvate
+/-0.01101 mM, reconstituted G2-EPSPS (by intein-mediated protein complementation), crude lysate from transformed Escherichia coli ER2799, malachite green dye assay
0.18
phosphoenolpyruvate
-
pH 7.0, recombinant enzyme, in presence of 100 mM KCl
0.23
phosphoenolpyruvate
wild-type, pH 7.0, temperature not specified in the publication
0.25
phosphoenolpyruvate
mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication
0.31
phosphoenolpyruvate
mutant P318R, pH 7.0, temperature not specified in the publication
0.32
phosphoenolpyruvate
mutant M425T, pH 7.0, temperature not specified in the publication
0.38
phosphoenolpyruvate
mutant N267S, pH 7.0, temperature not specified in the publication
0.525
phosphoenolpyruvate
mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication
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
43.6
phosphoenolpyruvate
-
recombinant enzyme, in crude extracts
0.049
shikimate 3-phosphate
in the presence of 1 mM NH4Cl and 10 mM KCl
0.109
shikimate 3-phosphate
in the presence of 1 mM NH4Cl and 100 mM KCl
additional information
additional information
-
kinetic parameters of native and diethyldicarbonate-inactivated enzyme
-
additional information
additional information
-
comparison of kinetic parameters from a variety of organism
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
pH 7.0, recombinant enzyme, in presence of 100 mM KCl
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
0.000012
5-enolpyruvylshikimate 3-phosphate
-
5-enpolpyruvylshikimate 3-phosphate ketal formation by hydrolysis of radiolabelled 5-enpolpyruvylshikimate 3-phosphate, pH 7.0, 25°C
0.23
5-enolpyruvylshikimate 3-phosphate
reverse reaction, in the presence of 50 mM KCl
1.2
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, mutant enzyme G99A
2.7
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, mutant strain L104P
7.4
5-enolpyruvylshikimate 3-phosphate
-
25°C, pH 7.0, wild-type enzyme
0.22
phosphate
reverse reaction, in the presence of 50 mM KCl
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
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
2
phosphoenolpyruvate
in the presence of 1 mM NH4Cl and 10 mM KCl
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
4.3
phosphoenolpyruvate
-
pH 7.0, recombinant enzyme, in presence of 100 mM KCl
12.8
phosphoenolpyruvate
in the presence of 1 mM NH4Cl and 100 mM KCl
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
26.7
phosphoenolpyruvate
wild-type, pH 7.0, temperature not specified in the publication
29.7
phosphoenolpyruvate
mutant G96A, in presence of 1 mM shikimate 3-phosphate
31.7
phosphoenolpyruvate
mutant N267S, pH 7.0, temperature not specified in the publication
32
phosphoenolpyruvate
C-terminal His6-tagged AroA, 50 mM KCl, cosubstrate: 3-phosphoshikimate
35
phosphoenolpyruvate
mutant M425T, pH 7.0, temperature not specified in the publication
43.3
phosphoenolpyruvate
mutant P318R, pH 7.0, temperature not specified in the publication
51.7
phosphoenolpyruvate
mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication
51.7
phosphoenolpyruvate
mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication
100
phosphoenolpyruvate
C-terminal His6-tagged AroA, 100 mM KCl, cosubstrate: 3-phosphoshikimate
additional information
5-enolpyruvylshikimate 3-phosphate
-
kat/KM: 1100000 M(-1)s(-1), mutant L104P
additional information
5-enolpyruvylshikimate 3-phosphate
-
kcat/KM: 3400000 M(-1)s(-1)
additional information
5-enolpyruvylshikimate 3-phosphate
-
kcat/KM: 660000 M(-1)s(-1), mutant G99A
additional information
phosphate
-
kcat/KM: 110 M(-1)s(-1), mutant L104P
additional information
phosphate
-
kcat/KM: 130 M(-1)s(-1), mutant G99A
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
83.3
phosphoenolpyruvate
mutant N267S, pH 7.0, temperature not specified in the publication
109.3
phosphoenolpyruvate
mutant M425T, pH 7.0, temperature not specified in the publication
115.9
phosphoenolpyruvate
wild-type, pH 7.0, temperature not specified in the publication
139.8
phosphoenolpyruvate
mutant P318R, pH 7.0, temperature not specified in the publication
206.7
phosphoenolpyruvate
mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication
206.7
phosphoenolpyruvate
mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000039 - 0.0018
(3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
0.00076 - 0.076
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
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 - 0.000063
(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
0.0000039
(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
0.00045
(3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
-
+/-70 nM
0.0018
(3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
+/-0.0006 mM
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
0.011
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
-
+/-0.002 mM
0.076
(3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
+/-0.009 mM
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
0.00003
(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
-
+/-6 nM
0.000063
(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
+/-15 nM
0.000048
glyphosate
-
wild type enzyme, at 28°C, pH not specified in the publication
0.00048
glyphosate
-
mutant enzyme A187T, at 28°C, pH not specified in the publication
0.0005
glyphosate
-
pH 7.0, 30°C, wild-type StaroA
0.0092
glyphosate
-
mutant enzyme T101A, at 28°C, pH not specified in the publication
0.0128
glyphosate
-
pH 7.0, 30°C, mutant StaroA-T42M
0.035
glyphosate
+/-0.00578 mM, reconstituted G2-EPSPS (by intein-mediated protein complementation), crude lysate from transformed Escherichia coli ER2799, malachite green dye assay
0.0495
glyphosate
+/-0.00317 mM, full-length G2 EPSPS, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
0.069
glyphosate
wild-type, pH 7.0, temperature not specified in the publication
0.08
glyphosate
mutant N267S, pH 7.0, temperature not specified in the publication
0.091
glyphosate
mutant M425T, pH 7.0, temperature not specified in the publication
0.1
glyphosate
-
+/-0.01 mM, in presence of 1 mM shikimate 3-phosphate and 0-500 mM inhibitor, bacterial extract
0.11
glyphosate
mutant P318R, pH 7.0, temperature not specified in the publication
0.15
glyphosate
mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication
0.16
glyphosate
mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication
0.2
glyphosate
-
+/-0.01 mM, mutant N130S, in presence of 1 mM shikimate 3-phosphate and 0-500 mM inhibitor, bacterial extract
0.48
glyphosate
-
mutant enzyme T101A/A187T, at 28°C, pH not specified in the publication
0.00012 - 0.00013
N-phosphonomethylglycine
-
isoenzymes I and II, vs. phosphoenolpyruvate
0.0003
N-phosphonomethylglycine
in the presence of 100 mM NH4Cl
0.0009
N-phosphonomethylglycine
-
vs. shikimate 3-phosphate, recombinant enzyme
0.005
N-phosphonomethylglycine
in the presence of 1 mM NH4Cl and 100 mM K+
0.008
N-phosphonomethylglycine
-
vs. 5-enolpyruvylshikimate 3-phosphate
0.098
N-phosphonomethylglycine
in the presence of 1 mM NH4Cl and 10 mM K+
0.54
N-phosphonomethylglycine
-
recombinant enzyme, in crude extracts
0.000015
shikimate 3-phosphate-5-carboxymethyl-(2R)-phosphonate
-
vs. 5-enolpyruvylshikimate-3-phosphate
0.00009
shikimate 3-phosphate-5-carboxymethyl-(2R)-phosphonate
-
vs. phosphate
0.0011
shikimate 3-phosphate-5-carboxymethyl-(2S)-phosphonate
-
vs. 5-enolpyruvylshikimate-3-phosphate
0.0021
shikimate 3-phosphate-5-carboxymethyl-(2S)-phosphonate
-
vs. phosphate
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
additional information
glyphosate
Ki/KM (phosphoenolpyruvate): 0.36, reconstituted G2-EPSPS (by intein-mediated protein complementation), crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
additional information
glyphosate
Ki/KM (phosphoenolpyruvate): 0.52, full-length G2 EPSPS, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00093
glyphosate
Malus domestica
-
wild type enzyme, at 28°C, pH not specified in the publication
0.0084
glyphosate
Malus domestica
-
mutant enzyme A187T, at 28°C, pH not specified in the publication
0.27
glyphosate
Malus domestica
-
mutant enzyme T101A, at 28°C, pH not specified in the publication
0.61
glyphosate
Brucella anthropi
wild-type, pH 7.0, temperature not specified in the publication
0.69
glyphosate
Brucella anthropi
mutant N267S, pH 7.0, temperature not specified in the publication
0.73
glyphosate
Brucella anthropi
mutant M425T, pH 7.0, temperature not specified in the publication
0.81
glyphosate
Brucella anthropi
mutant P318R, pH 7.0, temperature not specified in the publication
0.91
glyphosate
Brucella anthropi
mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication
0.92
glyphosate
Brucella anthropi
mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication
8
glyphosate
Pseudomonas stutzeri
-
+/-0.5 mM, in presence of 1 mM shikimate 3-phosphate and 0-500 mM inhibitor, bacterial extract
20
glyphosate
Pseudomonas stutzeri
-
+/-0.2 mM, mutant N130S, in presence of 1 mM shikimate 3-phosphate and 0-500 mM inhibitor, bacterial extract
55
glyphosate
Malus domestica
-
mutant enzyme T101A/A187T, at 28°C, pH not specified in the publication
additional information
glyphosate
Escherichia coli
more than 10 mM for mutant G96A/A183T
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0058
1.26
-
reverse reaction, i.e. phosphate + 5-enolpyruvylshikimate 3-phosphate
18
21.1
4.48
+/-0.79 micromol/min/mg, reconstituted G2-EPSPS (by intein-mediated protein complementation), mean specific activity, crude lysate from transformed Escherichia coli ER2799, malachite green dye assay
4.761
+/-0.92 micromol/min/mg, reconstituted G2-EPSPS (by intein-mediated protein complementation), maximum velocity, crude lysate from transformed Escherichia coli ER2799, malachite green dye assay
62
7.12
+/-0.13 micromol/min/mg, full-length G2 EPSPS, mean specific activity, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
7.24
+/-0.16 micromol/min/mg, full-length G2 EPSPS, maximum velocity, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay
8.5
0.0058
-
recombinant enzyme, activity in crude extracts
0.0058
-
wild-type enzyme, cell exract
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
-
phosphate + 5-enolpyruvylshikimate 3-phosphate, 2 maxima at pH 5.6 and pH 7.6
7.5
7.6
-
phosphate + 5-enolpyruvylshikimate 3-phosphate, 2 maxima, at pH 5.6 and pH 7.6
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
the enzyme activity is maintained at a pH range of 5.0-9.0, but lost abruptly at pH below 5.0 and above 9.0
5.5 - 8
-
more than 80% of the activity is retained between pH 5.5 and pH 8.0
5.5 - 8.7
-
approx. half-maximal activity at pH 5.5 and 8.7, phosphate + 5-enolpyruvylshikimate 3-phosphate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 60
-
the enzyme retains 20% of its activity at 0°C and 60°C, respectively, and shows about 45% activity at 20°C and about 90% at 40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacteria ATX1398
selected from soil by its ability to grow in presence of the herbicide glyphosate
-
-
brenda
transgenic Brassica napus x Brassica juncea outcrossing are examined
-
-
brenda
enzyme exists in 2 forms: one form is a monofunctional 59000 Da enzyme, the other form constitutes a single domain of the multifunctional 165000 Da arom protein
-
-
brenda
selected from soil by its ability to grow in presence of the herbicide glyphosate
-
-
brenda
formerly Aerobacter aerogenes, glyphosate sensitive and resistant strains
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
putative N-terminal transit peptide consisting of 70 amino acids which is present in other plant EPSP synthases and lacking in the bacterial enzyme
brenda
-
putative N-terminal transit peptide consisting of 70 amino acids which is present in other plant EPSP synthases and lacking in the bacterial enzyme
-
brenda
-
multifunctional enzyme form i.e. single domain of arom protein
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
transgene inheritance and quantification upon wild Brassica juncea x transgenic Brassica napus outcrossing from three backcross generations and their progenies are examined using real-time PCR. Under in vitro conditions, a stable inheritance and similar cp4 epsps copy number between different generations and their progenies are shown. A marginally higher copy number is observed when Brassica juncea is used as the paternal as compared to when it is used as maternal parent
metabolism
physiological function
metabolism
-
key enzyme in the shikimic acid pathway for biosynthesis of aromatic amino acids, lignin, and defensive compounds
metabolism
the enzyme activates the expression of MYB021 and the phenylpropanoid pathway
physiological function
enzyme is able to restore the growth of the Escherichia coli mutant ER2799, with the 5-enolpyruvylshikimate-3-phosphate synthase gene deleted from its genome, on an M9 minimal medium containing 60 mM glyphosate
physiological function
the enzyme in its regulatory form and hAT transposase form a transcriptional hierarchy regulating phenylpropanoid pathway and lignin biosynthesis in Populus
physiological function
-
enzyme is able to restore the growth of the Escherichia coli mutant ER2799, with the 5-enolpyruvylshikimate-3-phosphate synthase gene deleted from its genome, on an M9 minimal medium containing 60 mM glyphosate
-
Show AA Sequence and Transmembrane Helices (43906 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105500
20400
C-terminal fragment (from Thr296) expressed in pKEB12, Western blot
290000
-
aromatic multifunctional enzyme protein, sedimentation equilibrium analysis
44000
45000
46430
46700
47000
47500
48000
-
mixture of monomers and dimers in the absence of NH4Cl, only monomers in the presence of NH4Cl, gel filtration
49000
50000
73000
overexpressed mature protein (47000 Da) with GST tag (26000 Da)
83000
50000
-
wild-type and mutants, SDS-PAGE after induced overexpression in Escherichia coli
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
homodimer
Limnospira fusiformis Hegewald 1976/83
-
-
-
homodimer
2 * 47500, calculated from amino acid sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch under oil method, using 100 mM bis-Tris propane pH 7.0, 100 mM potassium bromide, 40% (w/v) PEG 8000
-
wild-type in presence of 5 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: 2PQB) or (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, PDB: 2PQC), and mutant A100G in presence of 5 mM inhibitor 2F-TI (PDB: 2PQD): 2F-TI-binding induces only slight shift of Glu354 side chain but substantial conformational change of 2F-TI molecule that is independent of residue 100 but mediated by residue Thr101 and due to rigidity of active site, RP-TI-binding induces slight movement of Glu354 side chain and occurs via salt bridge with residue Arg128 but does not alter enzymes backbone compared to the shikimate 3-phosphate bound enzyme, crystals: space group P2(1), unit cell parameters: a: 62.8-63.4, b: 44.9-45.0, c: 77.1-77.6, beta: 106.1-106.3°, hanging-drop vapour-diffusion, ammonium sulfate conditions, molecular replacement using PDB: 2GG6 as model, co-crystallization with (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) not succeeded, docking of SP-TI into substrate- or inhibitor-bound structures indicates low electrostatic interactions between enzyme and inhibitor
molecular docking using known structures of EPSPS in complex with (R)-phosphonate analogue of the tetrahedral reaction intermediate
-
three-dimensional structure modeling of mutations P318R and M425T. Results indicate that the enzyme's lower hemispheres upper surface is possibly another important region for glyphosate resistance
hanging drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 0.2 M NaCl, 20% (w/v) PEG 3350, and 5-10% (v/v) glycerol
sitting drop vapor diffusion method, using either 0.1 M trisodium citrate (pH 4.0) and 0.8 M ammonium sulfate (unliganded-open enzyme form) or 4.3 M NaCl and 0.1 M HEPES (pH 7.5) (unliganded-closed enzyme form) or 0.1 M Bis-Tris (pH 6.5) and 25% (w/v) PEG3350 (in complex with 3-phosphoshikimate and glyphosate) or 0.2 M ammonium sulfate, 0.1 M HEPES (pH 7.5), and 25% (w/v) PEG 3350 (in complex with K+, phosphate and 3-phosphoshikimate)
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
restrained-based, molecular modelling; open conformation model of apoenzyme generated based on coordinates from PDB: 2BJB (MtEPSPS), closed conformation model of enzyme/3-phosphoshikimate/glyphosate complex generated based on PDB: 1G6S
molecular modelling, two similar globular, inside-out alpha-beta-barrel domains connected by a two-stranded hinge, substrates bind at the inter-domain cleft
-
sitting drop vapor diffusion method, using 0.2 M MgCl, 0.1 M HEPES (pH 7.5), and 25% (w/v) PEG 3350
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A100G
G100A
-
the mutant has a 30fold increase in the IC50 value for glyphosate and slightly reduced specific activity compared to the wild type enzyme
G100A
-
the mutant has a 30fold increase in the IC50 value for glyphosate and slightly reduced specific activity compared to the wild type enzyme
-
agriculture
-
glyphosate resistance is correlated with the degree of enzyme over-expression in plants
DELTAN1-22
E145G/N163H/N267S/P318R/M377V/M425T/P438L
mutant is able to restore the growth of the Escherichia coli mutant ER2799, with the 5-enolpyruvylshikimate-3-phosphate synthase gene deleted from its genome, on an M9 minimal medium containing 300 mM glyphosate. The effectiveness of amino acid alterations N267S, P318R, and M245T on glyphosate tolerance is in the decreasing order P318R, M425T, N267S
M425T
mutation identified in a multiple mutant enzyme resistant to glyphosate
N267S
mutation identified in a multiple mutant enzyme resistant to glyphosate
N267S/P318R/M425T
mutant enzyme shows high tolerance against glyphosate
P318R
mutation identified in a multiple mutant enzyme resistant to glyphosate
P106S
T102I/P106S
-
the mutant shows very high-level (2647fold) in vitro resistance to glyphosate relative to the wild type enzyme
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
D242A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
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
D348A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
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
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
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
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
T355S
agriculture
the enzyme is efficiently utilized to develop transgenic glyphosate-tolerant crops
A187T
-
the mutation alters glyphosate resistance and slightly reduces enzyme activity
T101A
-
the mutation alters glyphosate resistance and strongly reduces enzyme activity
T101A/A187T
-
the mutation alters glyphosate resistance and reduces enzyme activity
agriculture
-
genetically engineered rice endogenous enzyme gene overexpressing 5-enolpyruvoylshikimate-3-phosphate synthase can increase glyphosate herbicide-resistance of cultivated rice. This type of enzyme transgene can enhance the fecundity of rice crop-weed hybrid offspring in the absence of glyphosate, stimulating great concerns over undesired environmental impacts of transgene flow to populations of wild relatives
P106L
P106L mutant has a high glyphosate resistance while retaining relatively high catalytic efficiency at low phosphoenolpyruvate concentrations. 3-fold increase in glyphosate resistance of Escherichia coli expressing the P106L mutant. Affinity of the P106L mutant for glyphosate and phosphoenolpyruvate is decreased about 70-fold and 4.6-fold, respectively, compared to wild-type
G99A
L104P
N130D
in a growth complementation assay no difference to wild-type
N130G
in a growth complementation assay no difference to wild-type
N130H
in a growth complementation assay no difference to wild-type
N130L
in a growth complementation assay no difference to wild-type
N130S
N130W
partial impaiment in growth complementation assay, mutant shows a significant decrease in resistance to glyphosate, Km (phosphoenolpyruvate): 0.025 mM
N130S
-
glyphosate resistance enhanced to 200 mM and glyphosate affinity reduced (2.5fold increase in IC50 and 2fold increase in Ki for glyphosate compared to wild-type) but similar catalytic activity as wild-type, generated by error-prone PCR
-
T38K/R40V/R222Q/S224V/I225V/Q226K
mutant with the c-strand of subdomain 3 and the f-strand of subdomain 5 substituted by the corresponding region of the Escherichia coli enzyme. The mutant enzyme exhibits greater sensitivity to glyphosate than the wild type with little change of affinity for substrates shikimate-3-phosphate and phosphoenolpyruvate
T38K/R40V/R222Q/S224V/I225V/Q226K
-
mutant with the c-strand of subdomain 3 and the f-strand of subdomain 5 substituted by the corresponding region of the Escherichia coli enzyme. The mutant enzyme exhibits greater sensitivity to glyphosate than the wild type with little change of affinity for substrates shikimate-3-phosphate and phosphoenolpyruvate
-
T42M
-
site-directed mutagenesis, the mutation is responsible for the glyphosate resistance and the low Km for phosphoenolpyruvate
food industry
-
the enzyme can be used for cultivation of glyphosate-tolerant plants
T103I/P107S
-
double mutant (47 kDa) which is widely used by genetic engineering to confer glyphosate tolerant properties, to various crops such as corn, cotton, canola, and soybean is assessed in terms of safety aspects: The expressed protein is innocuous. The double mutant enzyme does not possess any of the properties associated with known toxins or allergens, a rapid degradation in simulated gastric and intestinal fluids, and no adverse effects in mice after intravenousor oral administration is shown
additional information
A100G
glyphosate-sensitive, compared to wild-type similar inhibition constants for (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, (3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid, and (3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
A100G
-
glyphosate-sensitive, compared to wild-type similar inhibition constants for (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, (3R,4S,5R)-4-hydroxy-5-[(2R)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid, and (3R,4S,5R)-4-hydroxy-5-[(2S)-1-hydroxy-1-oxo-2-phosphono-propan-2-yl]oxy-3-phosphonooxy-cyclohexene-1-carboxylic acid
-
DELTAN1-22
-
lacking N-terminal 22 residues including critical amino acid Lys20, fails to provide glyphosate tolerance compared to full-length enzyme when transformed in glyphosate-sensitive Escherichia coli DH5alpha and XL1 Blue
DELTAN1-22
Bacteria ATX1398
-
lacking N-terminal 22 residues including critical amino acid Lys20, fails to provide glyphosate tolerance compared to full-length enzyme when transformed in glyphosate-sensitive Escherichia coli DH5alpha and XL1 Blue
-
P106S
-
the mutant shows high in vitro resistance to glyphosate relative to the wild type enzyme
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
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
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
T355S
mutation results in a catalytically more efficient glyphosate-resistant enzyme
T355S
-
mutation results in a catalytically more efficient glyphosate-resistant enzyme
-
G99A
-
KM-value for 5-enolpyruvylshikimate 3-phosphate is 86% of the wild-type value, KM-value for phosphate is 1.3fold higher than wild-type value. Turnover-number for 5-enolpyruvylshikimate 3-phosphate is 6.2fold higher than wild-type value, turnover-number for phosphate is 5.4fold lower than wild-type value
G99A
-
similar substrate affinities and decreased turnover compared to wild-type, fails to complement aroA auxotrophy in transformed Escherichia coli
L104P
-
KM-value for 5-enolpyruvylshikimate 3-phosphate is 1.14fold higher than the wild-type value, KM-value for phosphate is 4.4fold higher than wild-type value. Turnover-number for 5-enolpyruvylshikimate 3-phosphate is 2.7fold lower than wild-type value, turnover-number for phosphate is 1.9fold lower than wild-type value
L104P
-
lower affinity to phosphate and decreased turnover compared to wild-type, fails to complement aroA auxotrophy in transformed Escherichia coli
N130S
-
glyphosate resistance enhanced to 200 mM and glyphosate affinity reduced (2.5fold increase in IC50 and 2fold increase in Ki for glyphosate compared to wild-type) but similar catalytic activity as wild-type, generated by error-prone PCR
N130S
in a growth complementation assay no difference to wild-type, Km (phosphoenolpyruvate): 0.032 mM
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
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, i.e. mutant construct aroA-M1, 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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
the enzyme is stable from pH 4.0 to 8.0 with more than 60% activity remaining after 1 h incubation
759163
5 - 9
the enzyme is stable over a broad range of pH 5.0-9.0, especially at pH 7.5, with more than 80% activity after 1 h incubation
739758
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
the enzyme has half-lives of 346, 131, 39 and 12 min at 30, 40, 50 and 60°C, respectively
30 - 90
-
the half-lives of the enzyme at 30, 50, 70 and 90°C are 630, 138, 24 and 9 min, respectively
45
-
isoenzyme I, 50% loss of activity after 20 min, isoenzyme II, 50% loss of activity after 60 min
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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
-
freezing inactivates, Polybuffer 74, operating range pH 7-4, 1 mM dithioerythritol stabilize
-
prolonged dialysis against 50 mM Tris-HCl buffer, pH 7.5, 0.1 mM DTT, 1 mM benzamidine hydrochloride, 5 mM EDTA, 1 mM PMSF, stable to
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, in Polybuffer 74 from Pharmacia, operating range pH 7-4, 1 mM dithioerythritol, at least 9 months
-
-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
-
4°C, ammonium sulfate precipitate, 4 months, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, anion exchange chromatography, gel filtration, chromatofocusing
-
ammonium sulfate, DEAE-cellulose, hydroxyapatite, phenylaggarose, Sephacryl S-200, isozymes I, II and III
-
from bacterial lysate by single step cobalt affinity chromatography followed by dialysis
-
from crude cell extracts by DEAE-sepharose anion-exchange chromatography (Pharmacia XK-16/40 column, elution with linear NaCl gradient), Superdex 200 gel filtration chromatography (Pharmacia Superdex 200 HR 10/30 column coupled to FPLC, pH 6.8), Resource Q anion-exchange chromatography (elution with linear NaCl gradient, pH 6.8)
-
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)
glyphosate insensitve strain, ammonium sulfate, heat treatment, DEAE-cellulose, Sephadex G-75, cellulose phosphate, chromatofocusing
-
His-Bind agarose resin column chromatography and Superdex 200 gel filtration
HisTrap nickel affinity column chromatography and HiPrep 26/60 Superdex gel filtration
Ni-NTA column chromatography
recombinant enzyme, ammonium sulfate, DEAE-Sephacel, phenyl-Sepharose, phosphocellulose chromatography
-
recombinant enzyme, ammonium sulfate, hydrophobic interaction chromatography, anion-exchange chromatography
using an anion exchange Q-Sepharose column, ammonium sulfate precipitation using an equilibrated phenyl Sepharose column
-
HisTrap nickel affinity column chromatography and HiPrep 26/60 Superdex gel filtration
HisTrap nickel affinity column chromatography and HiPrep 26/60 Superdex gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified by 3 and 5 RACE on total RNA according to an EST found in Dunaliella salina cDNA library, cloned into pMD18-T for sequencing, cloned in pGEX-4T-1 for expression as mature protein (lacking N-terminal 70 amino acids long transit peptide) in Escherichia coli JM109 or EPSP synthase gene deleted Escherichia coli strain ER2799
by PCR from genomic DNA of strain A1501 and error-prone PCR on full-length EPSPS gene, in pACYC184 for transformation and complementation analyses in aroA-inactive mutant Escherichia coli AKM4188, or in pET-28a for expression in Escherichia coli BL21
-
coding sequence of CaEPSPS gene is successfully subcloned in a plasmid-Escherichia coli system (pET-32a), and the cells containing the plasmid carrying the CaEPSPS gene exhibit enhanced tolerance to herbicide glyphosate, compared to the control
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain BL21 (DE3) and Arabidopsis thaliana
-
expressed in Escherichia coli strain BL21 and Isatis indigotica hairy roots
-
expression in Escherichia coli
expression 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 Escherichia coli strain XL1-Blue
-
expression 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 Escherichia coli strain 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
-
expression of wild-type and chimeras of Salmonella typhimurium and Escherichia coli mutant enzymes in Escherichia coli
-
expression of wild-type and R24D, P105S, H385L mutant enzymes in Escherichia coli
-
from genomic DNA, in cosmid vector for phage packaging and transfection in Escherichia coli JM101 or in vitro transposon mutagenesis and transformation in Escherichia coli XL1 Blue MRF, in pAX306 for transformation of Escherichia coli DH5alpha and XL1 Blue MRF, in pRSF1b for inducible expression in Escherichia coli, in pSB11 shuttle vector for integration into Agrobacterium tumefaciens LBA4404 (already harbouring pSB1) and subsequent transformation of positive Agrobacterium strains in maize embryo for generation of transgenic plants
-
from genomic DNA, in pUC18 for complementation studies in Escherichia coli strain AB2829 (aroA auxotroph), in pTrc99A for inducible expression in Escherichia coli AB 2829
-
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
-
mutant G96A is expressed in Escherichia coli BL21 cells and Oryza sativa
N-terminal fragment (until Phe295) of G2 EPSPS or the complete gene in pMEB2 (N-terminal of splicing domain of of DnaE intein, strain PCC6803) and C-terminus (from Thr296) of G2 EPSPS in pKEB12 (C-terminal of splicing domain of DnaE intein, strain PCC6803) for intein-mediated protein complementation and expression in Escherichia coli strain ER2799, complete G2 EPSPS gene, N-terminal and C-terminal fragments in pBI121 for introduction into Agrobacterium sp. strain LBA4404 and transformation in Nicotiana tabacum variant NC89 for generation of transgenic plants
overexpression in Escherichia coli
overexpression of wild-type, His-tagged wild-type and several mutant enzymes in Escherichia coli
subcloned from bacteriophage lambdapserC into multicopy plasmid pAT153 with subsequent transformation of Escherichia coli AB2829 CGSC2829 cells
-
wild-type and mutants in pET-24d for expression in Escherichia coli BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is upregulated by methyl jasmonate, salicylic acid and abscisic acid treatment
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
pellet from 80% (w/v) ammonium sulfate solution, resolubilization and dialysis against 5 mM sodium phosphate, pH 6.9
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
drug development
synthesis
agriculture
Arabidopsis thaliana transgenic plants expressing mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L grow well in presence of 0.75 mM glyphosate, whereas Arabidopsis thaliana plants expressing wild-type enzyme grow only in presence of 0.25 mM glyphosate
agriculture
transgenic Arabidopsis thaliana plants expressing the enzyme from Bacillus cereus germinate well in presence of 1 mM glyphosate, while control plants do not germinate at 0.2 mM
agriculture
transgenic Arabidopsis thaliana plants expressing the enzyme from Halothermothrix orenii are more resistant to glyphosate exposure than transgenic plants expressing the Escherichia coli enzyme and control plants
agriculture
transgenic Arabidopsis thaliana plants expressing the enzyme from Pseudomonas fluorescens are more resistant to glyphosate exposure compared with wild-type
agriculture
transgenic Arabidopsis thaliana plants expressing the enzyme from Rahnella aquatilis are more resistant to glyphosate exposure than plants expressing the Escherichia coli enzyme
agriculture
-
transgenic Arabidopsis thaliana plants expressing the enzyme from Rahnella aquatilis are more resistant to glyphosate exposure than plants expressing the Escherichia coli enzyme
-
agriculture
-
transgenic Arabidopsis thaliana plants expressing the enzyme from Halothermothrix orenii are more resistant to glyphosate exposure than transgenic plants expressing the Escherichia coli enzyme and control plants
-
biotechnology
strain PCC6803 DnaE intein N-terminal and C-terminal splicing domains can reconstitute EPSPS activities and glyphosate resistance in plant
biotechnology
-
strain PCC6803 DnaE intein N-terminal and C-terminal splicing domains can reconstitute EPSPS activities and glyphosate resistance in plant
-
biotechnology
Bacteria ATX1398
-
conferring glyphosate tolerance in transgenic crop plants
-
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
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
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
drug development
-
more experimental data needed for effective structure-based drug design
drug development
-
protonated enolpyruvylshikimate 3-phosphate (cation) intermediate as potential target for inhibitor design
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
enzyme is a target for development and synthesis of antimicrobial drugs
synthesis
-
enzyme is a target for development and synthesis of antimicrobial drugs
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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
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Lambert, J.M.; Boocock, M.R.; Coggins, J.R.
The 3-dehydroquinate synthase activity of the pentafunctional arom enzyme complex of Neurospora crassa is Zn2+-dependent
Biochem. J.
226
817-829
1985
Neurospora crassa, Neurospora crassa 74-OR23-1A
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Gaertner, F.H.
Purification of two multienzyme complexes in the aromatic-tryptophan pathway of Neurospora crassa
Arch. Biochem. Biophys.
151
277-284
1972
Neurospora crassa
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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
brenda
Lewendon, A.; Coggins, J.R.
Purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli
Biochem. J.
213
187-191
1983
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Sost, D.; Chulz, A.; Amrhein, N.
Characterizaation of a glyphosphate-insensitive 5-enolpyruvylshikimic acid-3-phosphate synthase
FEBS Lett.
173
238-242
1984
Klebsiella pneumoniae
-
brenda
Steinrcken, H.C.; Amrhein, N.
5-Enolpyruvylshikimate-3-phosphate synthase of Klebsiella pneumoniae. 1. Purification and properties
Eur. J. Biochem.
143
341-349
1984
Klebsiella pneumoniae
brenda
Steinrcken, H.C.; Amrhein, N.
5-Enolpyruvylshikimate-3-phosphate synthase of Klebsiella pneumoniae 2. Inhibition by glyphosate [N-(phosphonomethyl)glycine]
Eur. J. Biochem.
143
351-357
1984
Klebsiella pneumoniae
brenda
Powell, H.A.; Kerby, N.W.; Rowell, P.; Mousdale, D.M.; Coggins, J.R.
Purification and properties of a glyphosphat-tolerant 5-enolpyruvylshikimate 3-phosphate synthase from the cyanobacterium Anabaena variabilis
Planta
188
484-490
1992
Trichormus variabilis
brenda
Mousdale, D.M.; Coggins, J.R.
Purification and properties of 5-enolpyruvylshikimate 3-phosphate synthase from sedlings of Pisum sativum L.
Planta
160
78-83
1984
Pisum sativum
brenda
Mousdale, D.M.; Coggins, J.R.
3-phosphoshikimate 1-carboxyvinyltransferase from Pisum sativum
Methods Enzymol.
142
348-354
1987
Lactuca sativa, Pisum sativum, Spinacia oleracea, Triticum aestivum, Zea mays
-
brenda
Alberg, D.G.; Bartlett, P.A.
Potent inhibition of 5-enolpyruvylshikimate-3-phosphate synthase by a reaction intermediate analogue
J. Am. Chem. Soc.
111
2337-2338
1989
Petunia x hybrida
-
brenda
Ream, J.E.; Steinrcken, H.C.; Porter, C.A.; Sikorski, J.A.
Purificatioin and properties of 5-enolpyruvylshikimate-3-phosphate synthase from dark-grown seedlings of Sorghum bicolor
Plant Physiol.
87
232-238
1988
Sorghum bicolor
brenda
Rubin, J.L.; Gaines, C.G.; Jensen, R.A.
Glyphosphate inhibition of 5-enolpyruvylshikimate 3-phosphate synthase from suspension-cultured cells of Nicotiana silvestris
Plant Physiol.
75
839-845
1984
Nicotiana sylvestris
brenda
Smart, C.C.; Johnning, D.; Mller, G.; Amrhein, N.
Selective overproduction of 5-enol-pyruvylshikimic acid 3-phosphate synthase in a plant cell culture which tolerates high doses of the herbicide glyphosate
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260
16338-16346
1985
Capnoides sempervirens
brenda
Smart, C.C.; Steinrcken, H.C.
Overproduction of 5-enolpryruvylshikimate 3-phosphate synthase in glyphosate-tolerant plant cell cultures
Plant Biol.
3
119-133
1987
Fagopyrum esculentum
-
brenda
Kishore, G.M.; Shah, D.M.
Amino acid biosynthesis inhibitors as herbicides
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57
627-663
1988
Pseudomonas sp.
brenda
Abdel-Meguid, S.S.; Smith, W.W.; Bild, G.S.
Crystallization of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli
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186
673
1985
Escherichia coli
brenda
Koshiba, T.
Organization of enzymes in the shikimate pathway of Phaseolus mungo seedlings
Plant Cell Physiol.
20
667-670
1979
Vigna radiata
-
brenda
Reinbothe, C.; Ortel, B.; Parthier, B.; Reinbothe, S.
Cytosolic and plastid forms of 5-enolpyruvylshikimate-3-phosphate synthase in Euglena gracilis are differentially expressed during light-induced chloroplast development
Mol. Gen. Genet.
245
616-622
1994
Euglena gracilis
brenda
Forlani, G.; Parisi, B.; Nielsen, E.
5-enol-Pyruvyl-shikimate-3-phosphate synthase from Zea Mays cultured cells. Purification and properties
Plant Physiol.
105
1107-1114
1994
no activity in mammals, Petunia x hybrida, Zea mays
brenda
Majumder, K.; Selvapandiyan, A.; Fattah, F.A.; Arora, N.; Ahmad, S.; Bhatnagar, R.K.
5-Enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis is an allosteric enzyme. Analysis of Arg24 -> Asp, Pro105 -> Ser and His385 -> Lys mutations suggests a hidden phosphoenolpyruvate-binding site
Eur. J. Biochem.
229
99-106
1995
Bacillus subtilis
brenda
Shuttleworth, W.A.; Evans, J.N.S.
The H385N mutant of 5-enolpyruvylshikimate-3-phosphate synthase: kinetics, fluorescence, and nuclear magnetic resonance studies
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334
37-42
1996
Escherichia coli
brenda
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
brenda
Du, W.; Wallis, N.G.; Mazzulla, M.J.; Chalker, A.F.; Zhang, L.; Liu, W.S.; Kallender, H.; Payne, D.J.
Characterization of Streptococcus pneumoniae 5-enolpyruvylshikimate 3-phosphate synthase and its activation by univalent cations
Eur. J. Biochem.
267
222-227
2000
Streptococcus pneumoniae (Q9S400), Streptococcus pneumoniae
brenda
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
brenda
Forlani, G.; Campani, A.
A dimeric 5-enol-pyruvyl-shikimate-3-phosphate synthase from the cyanobacterium Spirulina platensis
New Phytol.
151
443-450
2001
Arthrospira platensis
brenda
Oliveira, J.S.; Pinto, C.A.; Basso, L.A.; Santos, D.S.
Cloning and Overexpression in Soluble Form of Functional Shikimate Kinase and 5-Enolpyruvylshikimate 3-Phosphate Synthase Enzymes from Mycobacterium tuberculosis
Protein Expr. Purif.
22
430-435
2001
Mycobacterium tuberculosis
brenda
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)
brenda
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)
brenda
Forlani, G.
Differential expression of 5-enol-pyruvyl-shikimate-3-phosphate synthase isoforms in elicitor-treated, cultured maize cells
Funct. Plant Biol.
29
1483-1490
2002
Zea mays
brenda
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
brenda
Baerson, S.R.; Rodriguez, D.J.; Tran, M.; Feng, Y.; Biest, N.A.; Dill, G.M.
Glyphosate-resistant goosegrass. Identification of a mutation in the target enzyme 5-enolpyruvylshikimate-3-phosphate synthase
Plant Physiol.
129
1265-1275
2002
Eleusine indica, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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)
brenda
Oliveira, J.S.; Mendes, M.A.; Palma, M.S.; Basso, L.A.; Santos, D.S.
One-step purification of 5-enolpyruvylshikimate-3-phosphate synthase enzyme from Mycobacterium tuberculosis
Protein Expr. Purif.
28
287-292
2003
Mycobacterium tuberculosis
brenda
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
brenda
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
brenda
Priestman, M.A.; Funke, T.; Singh, I.M.; Crupper, S.S.; Schonbrunn, E.
5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate
FEBS Lett.
579
728-732
2005
Staphylococcus aureus
brenda
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
brenda
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
brenda
Borges, J.C.; Pereira, J.H.; Vasconcelos, I.B.; dos Santos, G.C.; Olivieri, J.R.; Ramos, C.H.; Palma, M.S.; Basso, L.A.; Santos, D.S.; de Azevedo, W.F.
Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis
Arch. Biochem. Biophys.
452
156-164
2006
Mycobacterium tuberculosis
brenda
Clark, M.E.; Berti, P.J.
Enolpyruvyl activation by enolpyruvylshikimate-3-phosphate synthase
Biochemistry
46
1933-1940
2007
Escherichia coli
brenda
Gong, Y.; Liao, Z.; Chen, M.; Guo, B.; Jin, H.; Sun, X.; Tang, K.
Characterization of 5-enolpyruvylshikimate 3-phosphate synthase gene from Camptotheca acuminata
Biol. Plant.
50
542-550
2006
Camptotheca acuminata (Q1M157)
-
brenda
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
brenda
Yi, Y.; Qiao, D.; Bai, L.; Xu, H.; Li, Y.; Wang, X.; Cao, Y.
Cloning, expression, and functional characterization of the Dunaliella salina 5-enolpyruvylshikimate-3-phosphate synthase gene in Escherichia coli
J. Microbiol.
45
153-157
2007
Dunaliella salina (A2T9R8), Dunaliella salina, Dunaliella salina 435 (A2T9R8)
brenda
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
brenda
Zhou, M.; Xu, H.; Wei, X.; Ye, Z.; Wei, L.; Gong, W.; Wang, Y.; Zhu, Z.
Identification of a glyphosate-resistant mutant of rice 5-enolpyruvylshikimate 3-phosphate synthase using a directed evolution strategy
Plant Physiol.
140
184-195
2006
Oryza sativa (Q93VK6), Oryza sativa
brenda
Vaithanomsat, P.; Brown, K.A.
Isolation and mutation of recombinant EPSP synthase from pathogenic bacteria Pseudomonas aeruginosa
Proc. Biochem.
42
592-598
2007
Pseudomonas aeruginosa
-
brenda
Dun, B.Q.; Wang, X.J.; Lu, W.; Zhao, Z.L.; Hou, S.N.; Zhang, B.M.; Li, G.Y.; Evans, T.C.; Xu, M.Q.; Lin, M.
Reconstitution of glyphosate resistance from a split 5-enolpyruvyl shikimate 3-phosphate synthase gene in Escherichia coli and transgenic tobacco
Appl. Environ. Microbiol.
73
7997-8000
2007
Pseudomonas fluorescens (A1Z0H6), Pseudomonas fluorescens G2 (A1Z0H6), Pseudomonas fluorescens G2
brenda
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)
brenda
Marques, M.R.; Vaso, A.; Neto, J.R.; Fossey, M.A.; Oliveira, J.S.; Basso, L.A.; dos Santos, D.S.; de Azevedo Junior, W.F.; Palma, M.S.
Dynamics of glyphosate-induced conformational changes of Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.19) determined by hydrogen-deuterium exchange and electrospray mass spectrometry
Biochemistry
47
7509-7522
2008
Mycobacterium tuberculosis (P9WPY5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPY5)
brenda
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
brenda
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)
brenda
Liang, A.; Sha, J.; Lu, W.; Chen, M.; Li, L.; Jin, D.; Yan, Y.; Wang, J.; Ping, S.; Zhang, W.; Wang, Y.; Lin, M.
A single residue mutation of 5-enoylpyruvylshikimate 3-phosphate synthase in Pseudomonas stutzeri enhances resistance to the herbicide glyphosate
Biotechnol. Lett.
30
1397-1401
2008
Pseudomonas stutzeri, Pseudomonas stutzeri A1501
brenda
Marques, M.R.; Pereira, J.H.; Oliveira, J.S.; Basso, L.A.; de Azevedo, W.F.; Santos, D.S.; Palma, M.S.
The inhibition of 5-enolpyruvylshikimate 3-phosphate synthase as a model for development of novel antimicrobials
Curr. Drug Targets
8
445-457
2007
Bacteria
brenda
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
brenda
Vande Berg, B.J.; Hammer, P.E.; Chun, B.L.; Schouten, L.C.; Carr, B.; Guo, R.; Peters, C.; Hinson, T.K.; Beilinson, V.; Shekita, A.; Deter, R.; Chen, Z.; Samoylov, V.; Bryant, C.T.; Stauffer, M.E.; Eberle, T.; Moellenbeck, D.J.; Carozzi, N.B.; Koziel, M.G.; Duck, N.B.
Characterization and plant expression of a glyphosate-tolerant enolpyruvylshikimate phosphate synthase
Pest Manag. Sci.
64
340-345
2008
Bacteria, plant, Bacteria ATX1398
brenda
Vaithanomsat, P.; Brown, K.A.
Isolation and mutation of recombinant EPSP synthase from pathogenic bacteria Pseudomonas aeruginosa
Process Biochem.
42
592-598
2007
Pseudomonas aeruginosa
-
brenda
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)
brenda
Song, X.; Munns, K.; Qiang, S.; Blackshaw, R.; Sharma, R.
Detection and quantification of 5 enolpyruvylshikimate-3-phosphate synthase (cp4 epsps) upon Brassica napus x Brassica juncea outcrossing using real-time PCR
Eur. Food Res. Technol.
228
939-944
2009
Brassica napus
brenda
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
brenda
Li, L.; Lu, W.; Han, Y.; Ping, S.; Zhang, W.; Chen, M.; Zhao, Z.; Yan, Y.; Jiang, Y.; Lin, M.
A novel RPMXR motif among class II 5-enolpyruvylshikimate-3-phosphate synthases is required for enzymatic activity and glyphosate resistance
J. Biotechnol.
144
330-336
2009
Pseudomonas stutzeri (A4VLZ3)
brenda
Herouet-Guicheney, C.; Rouquie, D.; Freyssinet, M.; Currier, T.; Martone, A.; Zhou, J.; Bates, E.E.; Ferullo, J.M.; Hendrickx, K.; Rouan, D.
Safety evaluation of the double mutant 5-enol pyruvylshikimate-3-phosphate synthase (2mEPSPS) from maize that confers tolerance to glyphosate herbicide in transgenic plants
Regul. Toxicol. Pharmacol.
54
143-153
2009
Zea mays
brenda
Tian, Y.S.; Xu, J.; Xiong, A.S.; Zhao, W.; Fu, X.Y.; Peng, R.H.; Yao, Q.H.
Improvement of glyphosate resistance through concurrent mutations in three amino acids of the Ochrobactrum 5-enopyruvylshikimate-3-phosphate synthase
Appl. Environ. Microbiol.
77
8409-8414
2011
Brucella anthropi (A6WUV8), Brucella anthropi
brenda
Tian, Y.S.; Xu, J.; Xiong, A.S.; Zhao, W.; Gao, F.; Fu, X.Y.; Peng, R.H.; Yao, Q.H.
Functional characterization of Class II 5-enopyruvylshikimate-3-phosphate synthase from Halothermothrix orenii H168 in Escherichia coli and transgenic Arabidopsis
Appl. Microbiol. Biotechnol.
93
241-250
2012
Halothermothrix orenii (B8CWX4), Halothermothrix orenii, Halothermothrix orenii H 168 (B8CWX4), Halothermothrix orenii H 168
brenda
Zhou, C.; Tian, Y.; Xu, Z.; Zhao, W.; Chen, C.; Bao, W.; Bian, L.; Cai, R.; Wu, A.
Identification of a new gene encoding 5-enolpyruvylshikimate-3-phosphate synthase using genomic library construction strategy
Mol. Biol. Rep.
39
10939-47
2012
Pseudomonas fluorescens (D7RH58)
brenda
Peng, R.H.; Tian, Y.S.; Xiong, A.S.; Zhao, W.; Fu, X.Y.; Han, H.J.; Chen, C.; Jin, X.F.; Yao, Q.H.
A novel 5-enolpyruvylshikimate-3-phosphate synthase from Rahnella aquatilis with significantly reduced glyphosate sensitivity
PLoS ONE
7
e39579
2012
Rahnella aquatilis (C9EGX2), Rahnella aquatilis, Rahnella aquatilis GR20 (C9EGX2)
brenda
Tian, Y.; Xu, J.; Han, J.; Zhao, W.; Fu, X.; Peng, R.; Yao, Q.
Complementary screening, identification and application of a novel class II 5-enopyruvylshikimate-3-phosphate synthase from Bacillus cereus
World J. Microbiol. Biotechnol.
29
549-557
2012
Bacillus cereus (F5A7Q0), Bacillus cereus
brenda
Sutton, K.A.; Breen, J.; Russo, T.A.; Schultz, L.W.; Umland, T.C.
Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii
Acta Crystallogr. Sect. F
72
179-187
2016
Acinetobacter baumannii, Acinetobacter baumannii 307-0294
brenda
Zhang, Y.; Yi, L.; Lin, Y.; Zhang, L.; Shao, Z.; Liu, Z.
Characterization and site-directed mutagenesis of a novel class II 5-enopyruvylshikimate-3-phosphate (EPSP) synthase from the deep-sea bacterium Alcanivorax sp. L27
Enzyme Microb. Technol.
63
64-70
2014
Alcanivorax sp., Alcanivorax sp. L27
brenda
Xing, X.J.; Tian, Y.S.; Peng, R.H.; Xu, J.; Zhao, W.; Yao, Q.H.; Sun, S.
Functional characterization of 5-enopyruvylshikimate-3-phosphate synthase from Alkaliphilus metalliredigens in transgenic Arabidopsis
J. Microbiol. Biotechnol.
24
1421-1426
2014
Alkaliphilus metalliredigens (A6TL04), Alkaliphilus metalliredigens
brenda
Yi, S.; Wu, G.; Lin, Y.; Hu, N.; Liu, Z.
Characterization of a new type of glyphosate-tolerant 5-enolpyruvyl shikimate-3-phosphate synthase from Isoptericola variabilis
J. Mol. Catal. B
111
1-8
2015
Isoptericola variabilis
-
brenda
Forlani, G.; Bertazzini, M.; Barillaro, D.; Rippka, R.
Divergent properties and phylogeny of cyanobacterial 5-enol-pyruvyl-shikimate-3-phosphate synthases: evidence for horizontal gene transfer in the Nostocales
New Phytol.
205
160-171
2015
Synechocystis sp., Calothrix sp., Calothrix sp. (K9PSG5), Fischerella muscicola, Gloeothece sp., Lyngbya sp., Desmonostoc muscorum, Nostoc sp., Nostoc sp. (K9QNN0), Nostoc sp. (Q3MAV9), Nostoc sp. (Q8YMB5), Oscillatoria sp., Oscillatoria sp. (K9TRT1), Oscillatoria sp. (K9VBD9), Synechococcus sp., Synechococcus sp. (B1XM36), Synechococcus sp. (B4WHQ7), Gloeobacter violaceus, Arthrospira sp., Arthrospira sp. (H1WFI3), Limnospira fusiformis, Fischerella thermalis, Stanieria sp. PCC 7301, Cylindrospermum licheniforme, Cylindrospermum majus PCC 7604, Tolypothrix sp. (A0A0D6KU47), Leptolyngbya boryana (A0A0P4UM05), Scytonema hofmannii (A0A139XBW5), Nostoc punctiforme (B2IYE4), Coleofasciculus chthonoplastes (B4VHX1), Microcystis aeruginosa (I4GHG6), Rivularia sp. PCC 7116 (K9RIB8), Chroococcidiopsis thermalis (K9TX81), Synechococcus elongatus (Q31RQ5), Synechococcus elongatus (Q5N2J9), Gloeothece sp. PCC 6909, Arthrospira sp. Compere 86.79, Desmonostoc muscorum PCC 7906, Oscillatoria sp. PCC 6304 (K9TRT1), Synechococcus sp. PCC 7335 (B4WHQ7), Nostoc sp. PCC 7413, Chroococcidiopsis thermalis PCC 7203 (K9TX81), Limnospira fusiformis Hegewald 1976/83, Leptolyngbya boryana PCC 6306 (A0A0P4UM05), Oscillatoria sp. PCC 7515, Nostoc sp. PCC 7937 (Q3MAV9), Calothrix sp. PCC 7102, Lyngbya sp. PCC 7419, Oscillatoria sp. PCC 7112 (K9VBD9), Scytonema hofmannii PCC 7110 (A0A139XBW5), Nostoc sp. PCC 6719, Nostoc sp. PCC 7120 (Q8YMB5), Microcystis aeruginosa PCC 7941 (I4GHG6), Arthrospira sp. PCC 8005 (H1WFI3), Synechococcus sp. PCC 6715, Synechococcus elongatus PCC 7942 (Q31RQ5), Arthrospira sp. PCC 9438, Coleofasciculus chthonoplastes PCC 7420 (B4VHX1), Calothrix sp. PCC 7507 (K9PSG5), Fischerella thermalis PCC 7521, Synechocystis sp. PCC 6701, Cylindrospermum licheniforme ATCC 29412, Arthrospira sp. PCC 9223, Fischerella muscicola PCC 73103
brenda
Wright, A.A.; Molin, W.T.; Nandula, V.K.
Distinguishing between weedy Amaranthus species based on intron one sequences from the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) gene
Pest Manag. Sci.
72
2347-2354
2016
Amaranthus hybridus, Amaranthus palmeri, Amaranthus spinosus, Amaranthus tuberculatus, Amaranthus viridis (A0A142K486), Amaranthus retroflexus (A0A142K487), Amaranthus blitoides (A0A142K488)
brenda
Tian, Y.S.; Xu, J.; Peng, R.H.; Xiong, A.S.; Xu, H.; Zhao, W.; Fu, X.Y.; Han, H.J.; Yao, Q.H.
Mutation by DNA shuffling of 5-enolpyruvylshikimate-3-phosphate synthase from Malus domestica for improved glyphosate resistance
Plant Biotechnol. J.
11
829-838
2013
Malus domestica
brenda
Yu, Q.; Jalaludin, A.; Han, H.; Chen, M.; Sammons, R.D.; Powles, S.B.
Evolution of a double amino acid substitution in the 5-enolpyruvylshikimate-3-phosphate synthase in Eleusine indica conferring high-level glyphosate resistance
Plant Physiol.
167
1440-1447
2015
Eleusine indica
brenda
Yi, S.Y.; Cui, Y.; Zhao, Y.; Liu, Z.D.; Lin, Y.J.; Zhou, F.
A novel naturally occurring class I 5-enolpyruvylshikimate-3-phosphate synthase from Janibacter sp. confers high glyphosate tolerance to rice
Sci. Rep.
6
19104
2016
Janibacter sp. (A3TGI7), Janibacter sp.
brenda
Wang, L.; Peng, R.; Tian, Y.; Han, J.; Zhao, W.; Wang, B.; Liu, M.; Yao, Q.
Characterization of a class II 5-enopyruvylshikimate-3-phosphate synthase with high tolerance to glyphosate from Sinorhizobium fredii
World J. Microbiol. Biotechnol.
30
2967-2973
2014
Sinorhizobium fredii (C3MC80), Sinorhizobium fredii, Sinorhizobium fredii NGR234 (C3MC80), Sinorhizobium fredii NGR234
brenda
Tan, X.L.; Othman, R.Y.; Teo, C.H.
Isolation and functional characterization of 5-enolpyruvylshikimate 3-phosphate synthase gene from glyphosate-tolerant Pseudomonas nitroreducens strains FY43 and FY47
3 Biotech
10
183
2020
Pseudomonas nitroreducens, Pseudomonas nitroreducens FY43, Pseudomonas nitroreducens FY47
brenda
Lee, J.H.; Choi, J.M.; Kim, H.J.
Crystal structure of 5-enolpyruvylshikimate-3-phosphate synthase from a psychrophilic bacterium, Colwellia psychrerythraea 34H
Biochem. Biophys. Res. Commun.
492
500-506
2017
Colwellia psychrerythraea (Q482G5), Colwellia psychrerythraea
brenda
Light, S.H.; Krishna, S.N.; Minasov, G.; Anderson, W.F.
An unusual cation-binding site and distinct domain-domain interactions distinguish class II enolpyruvylshikimate-3-phosphate synthases
Biochemistry
55
1239-1245
2016
Coxiella burnetii (Q83E11), Coxiella burnetii, Vibrio cholerae serotype O1 (Q9KRB0), Coxiella burnetii RSA 493 (Q83E11), Vibrio cholerae serotype O1 ATCC 39315 (Q9KRB0)
brenda
Liu, F.; Cao, Y.
Expression of the 5-enoylpyruvylshikimate-3-phosphate synthase domain from the Acremonium sp. aroM complex enhances resistance to glyphosate
Biotechnol. Lett.
40
855-864
2018
Acremonium sp.
brenda
Yu, J.; Zhang, Y.; Ning, S.; Ye, Q.; Tan, H.; Chen, R.; Bu, Q.; Zhang, R.; Gong, P.; Ma, X.; Zhang, L.; Wei, D.
Molecular cloning and metabolomic characterization of the 5-enolpyruvylshikimate-3-phosphate synthase gene from Baphicacanthus cusia
BMC Plant Biol.
19
485
2019
Strobilanthes cusia
brenda
Wang, L.; Peng, R.; Tian, Y.; Gao, J.; Wang, B.; Yao, Q.
A thermostable 5-enolpyruvylshikimate-3-phosphate synthase from Thermotoga maritima enhances glyphosate tolerance in Escherichia coli and transgenic Arabidopsis
Extremophiles
23
659-667
2019
Thermotoga maritima
brenda
Matthews, B.A.; Launis, K.L.; Bauman, P.A.; Juba, N.C.
Double-mutated 5-enol pyruvylshikimate-3-phosphate synthase protein expressed in MZHG0JG corn (Zea mays L.) has no impact on toxicological safety and nutritional composition
J. Agric. Food Chem.
65
8459-8465
2017
Zea mays
brenda
Liu, F.; Cao, Y.P.
Improvement of glyphosate resistance through concurrent mutations in three amino acids of the Pantoea sp. 5-enolpyruvylshikimate-3-phosphate synthase
J. Microbiol. Biotechnol.
28
1384-1390
2018
Pantoea sp.
brenda
Xie, M.; Muchero, W.; Bryan, A.C.; Yee, K.; Guo, H.B.; Zhang, J.; Tschaplinski, T.J.; Singan, V.R.; Lindquist, E.; Payyavula, R.S.; Barros-Rios, J.; Dixon, R.; Engle, N.; Sykes, R.W.; Davis, M.; Jawdy, S.S.; Gunter, L.E.; Thompson, O.; DiFazio, S.P.; Evans, L.M.; Winkeler, K.; Collins, C.; Schmutz, J.; Guo, H.
A 5-enolpyruvylshikimate 3-phosphate synthase functions as a transcriptional repressor in Populus
Plant Cell
30
1645-1660
2018
Populus trichocarpa (A0A2K1XRJ2)
brenda
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)
-
brenda
Yi, D.; Ma, L.; Lin, M.; Li, C.
Development of glyphosate-resistant alfalfa (Medicago sativa L.) upon transformation with the GR79Ms gene encoding 5-enolpyruvylshikimate-3-phosphate synthase
Planta
248
211-219
2018
uncultured soil bacterium
brenda
Yang, X.; Beres, Z.T.; Jin, L.; Parrish, J.T.; Zhao, W.; Mackey, D.; Snow, A.A.
Effects of over-expressing a native gene encoding 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) on glyphosate resistance in Arabidopsis thaliana
PLoS ONE
12
e0175820
2017
Arabidopsis thaliana
brenda
Yang, X.; Li, L.; Jiang, X.; Wang, W.; Cai, X.; Su, J.; Wang, F.; Lu, B.R.
Genetically engineered rice endogenous 5-enolpyruvoylshikimate-3-phosphate synthase (epsps) transgene alters phenology and fitness of crop-wild hybrid offspring
Sci. Rep.
7
6834
2017
Oryza sativa
brenda
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