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2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase

This is an abbreviated version!
For detailed information about 3-phosphoshikimate 1-carboxyvinyltransferase, go to the full flat file.

Word Map on EC 2.5.1.19

Reaction

phosphoenolpyruvate
+
3-phosphoshikimate
=
phosphate
+
5-O-(1-carboxyvinyl)-3-phosphoshikimate

Synonyms

3-enolpyruvylshikimate 5-phosphate synthase, 3-enolpyruvylshikimic acid-5-phosphate synthetase, 3-phosphoshikimate 1-carboxyvinyl-transferase, 3-phosphoshikimate 1-carboxyvinyltransferase, 3-phosphoshikimate-1-carboxyvinyl-transferase, 5'-enolpyruvylshikimate-3-phosphate synthase, 5-enol pyruvylshikimate 3-phosphate synthase, 5-enol-pyruvyl-shikimate-3-phosphate synthase, 5-enol-pyruvylshikimate 3-phosphate synthase, 5-enol-pyruvylshikimate-3-phosphate synthase, 5-enolpyruvyl-3-phosphoshikimate synthase, 5-enolpyruvylshikimate 3-phosphate synthase, 5-enolpyruvylshikimate-3-phosphate synthase, 5-enolpyruvylshikimate-3-phosphate synthetase, 5-enolpyruvylshikimate-3-phosphoric acid synthase, 5-enolpyruvylshikimate-3phosphate synthase, 5-enolpyruvylshikimic acid-3-phosphate synthase, 5-enopyruvylshikimate-3-phosphate synthase, 5-enoylpyruvylshikimate 3-phosphate synthase, 5-enoylpyruvylshikimate-3-phosphate synthase, A1501 EPSPS, AM79, AroA, AroA(1398), AroA(A1501), AroA1398, CaEPSPS, cp4 epsps, DsaroA, Dunaliella salina 5-enolpyruvylshikimate-3-phosphate synthase, Dunaliella salina EPSP synthase, E. coli EPSPS, EcaroA, enolpyruvylshikimate 3-phosphate synthase, enolpyruvylshikimate phosphate synthase, enolpyruvylshikimate-3-phosphate synthase, EPSP synhthase, EPSP synthase, EPSPS, G2 5-enolpyruvyl shikimate 3-phosphate synthase, G2 EPSPS, GR79Ms, maize EPSP synthase, maize EPSPS, mEPSPS, More, Mt EPSPS, Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase, Potri.002G146400, StaroA, synthase, 5-enolpyruvoylshikimate 3-phosphate

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.19 3-phosphoshikimate 1-carboxyvinyltransferase

Engineering

Engineering on EC 2.5.1.19 - 3-phosphoshikimate 1-carboxyvinyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
L105P
-
the mutant shows 20% catalytic activity compared to 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
-
L105P
-
the mutant shows 20% catalytic activity compared to wild type enzyme
-
agriculture
-
glyphosate resistance is correlated with the degree of enzyme over-expression in plants
H385L
-
0.2% of wild-type activity, 2fold activation at 100 mM NH4Cl
H385N
-
6% of wild-type activity
P105S
-
69% of wild-type activity, 8fold activation at 100 mM NH4Cl
R24D
-
0.8% of wild-type activity, 2fold activation at 100 mM NH4Cl
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
P381L
-
similiar glyphosate sensitivity like wild-type
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
D49A
41% of wild-type 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/A183T
H385A
K340A
2.4% of wild-type activity
K411A
10.4% of wild-type activity
N94A
50% of wild-type activity
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
Q171A
1.7% of wild-type activity
R100A
-
site-directed mutagenesis, the mutation is responsible for the high increase in activity
R100M
0.2% of wild-type activity
R124A
19.6% of wild-type activity
R27A
binding of shikimate 3-phosphate is abolished
R344K
31.7% of wild-type activity
R344M
16.3% of wild-type activity
R386M
15.8% of wild-type 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
Y200F
1% of wild-type activity
T355S
agriculture
the enzyme is efficiently utilized to develop transgenic glyphosate-tolerant crops
G96A
-
glyphosate-insensitive
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
G97A/T98I/P102S
-
the mutations significantly improve glyphosate resistance
L104P
A242V
-
the mutation leads to sensitivity to 8.768% glyphosate
A329T
-
the mutation leads to sensitivity to 8.768% glyphosate
G292C
-
the mutation leads to sensitivity to 8.768% glyphosate
G292S
-
the mutation does not affect sensitivity to glyphosate
L184F
-
the mutation leads to sensitivity to 8.768% glyphosate
L35F
-
the mutation leads to sensitivity to 8.768% glyphosate
N265S
-
the mutation leads to sensitivity to 8.768% glyphosate
P71L
-
the mutation leads to sensitivity to 8.768% glyphosate
R21C
-
the mutation leads to sensitivity to 8.768% glyphosate
T258A
-
the mutation leads to sensitivity to 8.768% glyphosate
A329T
-
the mutation leads to sensitivity to 8.768% glyphosate
-
G292S
-
the mutation does not affect sensitivity to glyphosate
-
N265S
-
the mutation leads to sensitivity to 8.768% glyphosate
-
R21C
-
the mutation leads to sensitivity to 8.768% glyphosate
-
T258A
-
the mutation leads to sensitivity to 8.768% glyphosate
-
A329T
-
the mutation leads to sensitivity to 8.768% glyphosate
-
G292S
-
the mutation does not affect sensitivity to glyphosate
-
N265S
-
the mutation leads to sensitivity to 8.768% glyphosate
-
R21C
-
the mutation leads to sensitivity to 8.768% glyphosate
-
T258A
-
the mutation leads to sensitivity to 8.768% glyphosate
-
M129W
no enzymatic activity
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
N130P
partial impaiment in growth complementation assay
N130S
N130W
partial impaiment in growth complementation assay, mutant shows a significant decrease in resistance to glyphosate, Km (phosphoenolpyruvate): 0.025 mM
P128R
no enzymatic activity
R127E
no enzymatic activity
R127K
no enzymatic activity
R131E
no enzymatic activity
R131K
no enzymatic activity
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
-
G96A
mutant with improved resistance towards glyphosate
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
G96A
-
mutant with improved resistance towards glyphosate
-
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