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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate

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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
push-pull mechanism of ring opening in which H388 breaks the O5-C1 bond by donating a proton, and simultaneously, K518 abstracts a proton from the C1 hydroxyl group
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
mechanism is based on an enediol intermediate
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
multistep catalytic mechanism, model including catalytically active amino acids
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
cis-endiol intermediate based mechanism with Glu97 acting as the catalytic base responsible for isomerization
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
on the basis of the calculations and simulations, a zwitterionic intermediate mechanism for the low-energy enzymatic reaction is proposed, involving both proton and hydride transfers
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase via cis-enediol-based mechanism with active site redundancy, structure-function analysis, overview. In the cis-enediol mechanism, a residue in the PGI enzyme active site acts as a base catalyst to remove a proton from C2 of glucose 6-phosphate, and the substrate forms a cis-enediol intermediate. The proton that is removed by the PGI base catalyst may exchange with protons from the solvent before being donated to C1 to form the product
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
the F6P to G6P isomerization reaction proceeds by a proton transfer mechanism between C-1 and C-2 of the substrates, concomitant with a proton transfer between O-1 and O-2, and involves a 1,2-cis-enediolate high-energy intermediate (HEI)
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
the F6P to G6P isomerization reaction proceeds by a proton transfer mechanism between C-1 and C-2 of the substrates, concomitant with a proton transfer between O-1 and O-2, and involves a 1,2-cis-enediolate high-energy intermediate (HEI)
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase via cis-enediol-based mechanism with active site redundancy, structure-function analysis, overview. In the cis-enediol mechanism, a residue in the PGI enzyme active site acts as a base catalyst to remove a proton from C2 of glucose 6-phosphate, and the substrate forms a cis-enediol intermediate. The proton that is removed by the PGI base catalyst may exchange with protons from the solvent before being donated to C1 to form the product
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase via cis-enediol-based mechanism with active site redundancy, structure-function analysis, overview. In the cis-enediol mechanism, a residue in the PGI enzyme active site acts as a base catalyst to remove a proton from C2 of glucose 6-phosphate, and the substrate forms a cis-enediol intermediate. The proton that is removed by the PGI base catalyst may exchange with protons from the solvent before being donated to C1 to form the product
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase via cis-enediol-based mechanism with active site redundancy, structure-function analysis, overview. In the cis-enediol mechanism, a residue in the PGI enzyme active site acts as a base catalyst to remove a proton from C2 of glucose 6-phosphate, and the substrate forms a cis-enediol intermediate. The proton that is removed by the PGI base catalyst may exchange with protons from the solvent before being donated to C1 to form the product
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
TM1385 from Thermotoga maritima functions as a phosphoglucose isomerase via cis-enediol-based mechanism with active site redundancy, structure-function analysis, overview. In the cis-enediol mechanism, a residue in the PGI enzyme active site acts as a base catalyst to remove a proton from C2 of glucose 6-phosphate, and the substrate forms a cis-enediol intermediate. The proton that is removed by the PGI base catalyst may exchange with protons from the solvent before being donated to C1 to form the product
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
alpha-D-glucose 6-phosphate
beta-D-fructose 6-phosphate
beta-D-fructofuranose 6-phosphate
alpha-D-glucose 6-phosphate
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Substrates: -
Products: -
r
beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
D-galactose
D-tagatose
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
D-Mannose 6-phosphate
D-Fructose 6-phosphate
fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
Glucose 6-phosphate
Fructose 6-phosphate
L-talose
L-tagatose
Substrates: best aldose substrate
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malonic dialdehyde
methylglyoxal
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Substrates: -
Products: -
r
additional information
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alpha-D-glucose 6-phosphate

beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate

beta-D-fructose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructose 6-phosphate
Substrates: -
Products: -
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alpha-D-glucose 6-phosphate
beta-D-fructose 6-phosphate
Substrates: -
Products: -
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beta-D-fructose 6-phosphate

alpha-D-glucose 6-phosphate
Substrates: -
Products: -
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beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
Substrates: -
Products: -
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beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
Substrates: -
Products: -
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beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
Substrates: -
Products: -
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beta-D-fructose 6-phosphate
alpha-D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate

D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Cassia coluteoides
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
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Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: the isomerization occurrs by a cis-enediol intermediate involving C-1 pro-R hydrogen of D-fructose 6-phosphate. The presence of metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate

D-mannose 6-phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate
D-mannose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate

D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Cassia coluteoides
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: the active site residues Lys58 and His388 might be involved in catalytic mechanism
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
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Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
Products: -
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D-Mannose 6-phosphate

D-Fructose 6-phosphate
Substrates: -
Products: -
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D-Mannose 6-phosphate
D-Fructose 6-phosphate
Substrates: -
Products: -
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Fructose 6-phosphate

Glucose 6-phosphate
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Substrates: r
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: r
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: r
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
-
Substrates: r
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
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Fructose 6-phosphate
Glucose 6-phosphate
-
Substrates: r
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: r
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
Products: -
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: r
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: r
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Fructose 6-phosphate
Glucose 6-phosphate
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Substrates: -
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Glucose 6-phosphate

Fructose 6-phosphate
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Substrates: -
Products: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
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Glucose 6-phosphate
Fructose 6-phosphate
-
Substrates: -
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Glucose 6-phosphate
Fructose 6-phosphate
-
Substrates: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
Products: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: -
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Glucose 6-phosphate
Fructose 6-phosphate
-
Substrates: r
Products: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
Products: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
Products: -
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Glucose 6-phosphate
Fructose 6-phosphate
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Substrates: r
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additional information

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Substrates: the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
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additional information
?
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Substrates: the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
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additional information
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Substrates: the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
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additional information
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Substrates: the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
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additional information
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Substrates: the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
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additional information
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Substrates: the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
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additional information
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Substrates: the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
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additional information
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Substrates: the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
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additional information
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Substrates: the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
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additional information
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Substrates: PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
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additional information
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Substrates: in addition to isomerase activity, PGI displays anomerase activity between anomers of D-glucopyranose 6-phosphate (alpha/beta-G6P) and between those of D-fructofuranose 6-phosphate (alpha/beta-F6P)
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additional information
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Substrates: the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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Substrates: the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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Substrates: in addition to isomerase activity, PGI displays anomerase activity between anomers of D-glucopyranose 6-phosphate (alpha/beta-G6P) and between those of D-fructofuranose 6-phosphate (alpha/beta-F6P)
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additional information
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Substrates: the enzyme is part of the glycolytic pathway
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additional information
?
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Substrates: glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
Products: -
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additional information
?
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Substrates: glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
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additional information
?
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Substrates: enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
Products: -
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additional information
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Substrates: enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
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additional information
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Substrates: glycolytic enzyme
Products: -
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additional information
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Substrates: enzyme of the oxidative pentose phosphate cycle
Products: -
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additional information
?
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Substrates: the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
Products: -
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additional information
?
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Substrates: the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
Products: -
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additional information
?
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Substrates: the catalytic isomerization activity of TM1385 is determined spectrophotometrically by NADPH absorbance at 340 nm. The coupled enzyme assay to measure TM1385 activity uses glucose-6-phosphate dehydrogenase (G6PDH) from Saccharomyces cerevisiae and the substrate fructose-6-phosphate. TM1385 computational docking with linear G6P substrate
Products: -
-
additional information
?
-
Substrates: the catalytic isomerization activity of TM1385 is determined spectrophotometrically by NADPH absorbance at 340 nm. The coupled enzyme assay to measure TM1385 activity uses glucose-6-phosphate dehydrogenase (G6PDH) from Saccharomyces cerevisiae and the substrate fructose-6-phosphate. TM1385 computational docking with linear G6P substrate
Products: -
-
additional information
?
-
Substrates: the catalytic isomerization activity of TM1385 is determined spectrophotometrically by NADPH absorbance at 340 nm. The coupled enzyme assay to measure TM1385 activity uses glucose-6-phosphate dehydrogenase (G6PDH) from Saccharomyces cerevisiae and the substrate fructose-6-phosphate. TM1385 computational docking with linear G6P substrate
Products: -
-
additional information
?
-
Substrates: the catalytic isomerization activity of TM1385 is determined spectrophotometrically by NADPH absorbance at 340 nm. The coupled enzyme assay to measure TM1385 activity uses glucose-6-phosphate dehydrogenase (G6PDH) from Saccharomyces cerevisiae and the substrate fructose-6-phosphate. TM1385 computational docking with linear G6P substrate
Products: -
-
additional information
?
-
Substrates: the catalytic isomerization activity of TM1385 is determined spectrophotometrically by NADPH absorbance at 340 nm. The coupled enzyme assay to measure TM1385 activity uses glucose-6-phosphate dehydrogenase (G6PDH) from Saccharomyces cerevisiae and the substrate fructose-6-phosphate. TM1385 computational docking with linear G6P substrate
Products: -
-
additional information
?
-
-
Substrates: probable role of the enzyme in starch biosynthesis in amyloplasts
Products: -
?
additional information
?
-
-
Substrates: glycolytic enzyme
Products: -
?
additional information
?
-
-
Substrates: glycolytic enzyme
Products: -
?
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alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
D-fructose 6-phosphate
D-glucose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
additional information
?
-
alpha-D-glucose 6-phosphate

beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
-
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
alpha-D-glucose 6-phosphate
beta-D-fructofuranose 6-phosphate
Substrates: -
Products: -
r
D-fructose 6-phosphate

D-glucose 6-phosphate
-
Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
Products: -
?
D-fructose 6-phosphate
D-glucose 6-phosphate
Substrates: -
Products: -
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate

D-fructose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
?
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
Products: -
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Substrates: -
Products: -
r
additional information

?
-
-
Substrates: the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
Products: -
?
additional information
?
-
-
Substrates: the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
Products: -
?
additional information
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-
-
Substrates: the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
Products: -
?
additional information
?
-
Substrates: the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
Products: -
?
additional information
?
-
Substrates: the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
Products: -
?
additional information
?
-
-
Substrates: the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
Products: -
?
additional information
?
-
-
Substrates: PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
Products: -
?
additional information
?
-
Substrates: the enzyme plays important roles in glycolysis and gluconeogenesis
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays important roles in glycolysis and gluconeogenesis
Products: -
?
additional information
?
-
-
Substrates: the enzyme is part of the glycolytic pathway
Products: -
?
additional information
?
-
-
Substrates: glycolytic enzyme
Products: -
?
additional information
?
-
-
Substrates: enzyme of the oxidative pentose phosphate cycle
Products: -
?
additional information
?
-
-
Substrates: probable role of the enzyme in starch biosynthesis in amyloplasts
Products: -
?
additional information
?
-
-
Substrates: glycolytic enzyme
Products: -
?
additional information
?
-
-
Substrates: glycolytic enzyme
Products: -
?
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1,5-Anhydroglucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-glucitol 6-phosphate dimethyl ester
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-mannitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-Deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-deoxyglucose 6-phosphate
-
-
5-deoxy-5-malonate-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinoate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinohydroxamate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinonohydroxamate
competitive, stable analogue of putative cis-endiol intermediate
5-phospho-D-arabinonohydroxamic acid
-
-
5-phosphoarabinonhydroxamic acid
6-phospho-2-deoxygluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phospho-D-gluconate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phospho-D-gluconoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-Phosphomannonate
Cassia coluteoides
-
with glucose 6-phosphate as substrate
Ca2+
slight inhibition at 1.5 mM
Co2+
10 mM, 59% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
dihydroxyacetone phosphate
-
-
Erythritol 4-phosphate
-
-
erythrose-4-phosphate
-
-
gluconate 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
GTP
-
competitive inhibitor, also compromises the autocrine motility factor function of the enzyme. The GTP-binding site partially overlaps with the catalytic site. In addition,GTP stabilizes the structure of PGI against heat- and detergent-induced denaturation. GTP is bound in a syn-conformation with the gamma-phosphate group located near the phosphate-binding loop and the ribose moiety positioned away from the active-site residues
insulin-like growth factor binding protein-3
-
both glycosylated and unglycosylated, binding and inhibition of enzyme
-
K+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
L-Sorbose 6-phosphate
-
-
L-xylulose 5-phosphate
-
-
Maleate
-
10 mM, 50% inhibition
malonate
-
10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
N,2,3,4,5-pentahydroxypentanamide
-
-
N-(5-phospho-D-arabinoyl)-1,4-lactone
-
N-(5-phospho-D-arabinoyl)-1-(1-methylimidazol-2-yl)methanamine
N-(5-phospho-D-arabinoyl)-1-(furan-2-yl)methanamine
N-(5-phospho-D-arabinoyl)-1-(imidazol-2-yl)methanamine
-
N-(5-phospho-D-arabinoyl)-1-(pyridin-2-yl)methanamine
N-(5-phospho-D-arabinoyl)-1-(thien-2-yl)methanamine
N-(5-phospho-D-arabinoyl)-2-(amino)ethanamine
N-(5-phospho-D-arabinoyl)-2-(methylsulfanyl)ethanamine
N-(5-phospho-D-arabinoyl)-2-(methylsulfonyl)ethanamine
N-(5-phospho-D-arabinoyl)-3-(aminomethyl)ethanolamine
N-(5-phospho-D-arabinoyl)-3-(imidazol-1-yl)propanamine
N-(5-phospho-D-arabinoyl)-hydroxamate
-
N-(5-phospho-D-arabinoyl)histamine
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
N-bromoacetylethanolamine phosphate
-
oxaloacetate
-
10 mM, 25% inhibition
oxoglutarate
-
10 mM, 20% inhibition
sedoheptulose 7-phosphate
5-phospho-D-arabinonate

-
5-phospho-D-arabinonate
5PAA
5-phospho-D-arabinonate
-
5PAA
5-phospho-D-arabinonate
-
5-phospho-D-arabinonate
competitive
5-phosphoarabinonhydroxamic acid

-
-
5-phosphoarabinonhydroxamic acid
competitive inhibition
6-phosphogluconate

-
6-phosphogluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phosphogluconate
-
0.2 mM, 52% inhibition
6-phosphogluconate
-
competitive
6-phosphogluconate
-
pH 7.6, 25°C
6-phosphogluconate
competitive inhibition
6-phosphogluconate
-
competitive
Agaricic acid

-
-
Agaricic acid
irreversible inhibition
Cd2+

10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
Cu2+

-
1 mM, about 40% inhibition
Cu2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate

10 mM, residual activities are 41% and 53% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-fructose 1,6-bisphosphate
-
D-Fructose 1-phosphate

2 mM, residual activities are 50% and 69% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-gluconate 6-phosphate

-
D-gluconate 6-phosphate
-
D-mannose 6-phosphate

1.25 mM, residual activities are 18% and 38% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
EDTA

-
-
EDTA
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
EDTA
-
the enzyme activity is completely diminished when the enzyme is heated at 70°C in the presence of 10 mM EDTA. Complete restoration of the enzyme activity is observed when the enzyme is incubated at room temperature in the presence of Zn2+
EDTA
10 mM, 78% inhibition, D-fructose 6-phosphate as substrate
erythrose 4-phosphate

-
erythrose 4-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
erythrose 4-phosphate
-
0.02 mM, 58% inhibition
erythrose 4-phosphate
-
activates enzyme form B with ribose 5-phosphate as substrate, inhibits activity of enzyme form A and B with glucose 6-phosphate as substrate, inhibits activity of enzyme form A with glucose 6-phosphate as substrate
erythrose 4-phosphate
-
competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
competitive inhibitor. Thermodynamic properties of the protein-inhibitor complex are explored by performing isothermal titration calorimetry that results in the Kd of 0.023 mM depicting that the active site for the Pseudomonas aeruginosa enzyme G6PI is conserved and is similar to the reported G6PI of other species
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
competitive
fructose 1,6-diphosphate

-
1 mM, 4% inhibition
fructose 1,6-diphosphate
-
-
fructose 1-phosphate

-
1 mM, 10% inhibition
Hg2+

-
1 mM, about 50% inhibition
Mn2+

10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
N-(5-phospho-D-arabinoyl)-1,4-lactone

-
-
N-(5-phospho-D-arabinoyl)-1,4-lactone
-
-
-
N-(5-phospho-D-arabinoyl)-1-(1-methylimidazol-2-yl)methanamine

-
N-(5-phospho-D-arabinoyl)-1-(1-methylimidazol-2-yl)methanamine
-
-
N-(5-phospho-D-arabinoyl)-1-(furan-2-yl)methanamine

-
N-(5-phospho-D-arabinoyl)-1-(furan-2-yl)methanamine
-
-
N-(5-phospho-D-arabinoyl)-1-(imidazol-2-yl)methanamine

-
-
N-(5-phospho-D-arabinoyl)-1-(imidazol-2-yl)methanamine
-
-
-
N-(5-phospho-D-arabinoyl)-1-(pyridin-2-yl)methanamine

-
N-(5-phospho-D-arabinoyl)-1-(pyridin-2-yl)methanamine
-
-
N-(5-phospho-D-arabinoyl)-1-(thien-2-yl)methanamine

-
N-(5-phospho-D-arabinoyl)-1-(thien-2-yl)methanamine
-
-
N-(5-phospho-D-arabinoyl)-2-(amino)ethanamine

-
N-(5-phospho-D-arabinoyl)-2-(amino)ethanamine
-
-
N-(5-phospho-D-arabinoyl)-2-(methylsulfanyl)ethanamine

-
N-(5-phospho-D-arabinoyl)-2-(methylsulfanyl)ethanamine
-
-
N-(5-phospho-D-arabinoyl)-2-(methylsulfonyl)ethanamine

-
N-(5-phospho-D-arabinoyl)-2-(methylsulfonyl)ethanamine
-
-
N-(5-phospho-D-arabinoyl)-3-(aminomethyl)ethanolamine

-
N-(5-phospho-D-arabinoyl)-3-(aminomethyl)ethanolamine
-
-
N-(5-phospho-D-arabinoyl)-3-(imidazol-1-yl)propanamine

-
N-(5-phospho-D-arabinoyl)-3-(imidazol-1-yl)propanamine
-
-
N-(5-phospho-D-arabinoyl)-hydroxamate

5PAH
-
N-(5-phospho-D-arabinoyl)-hydroxamate
-
5PAH
-
N-(5-phospho-D-arabinoyl)histamine

-
N-(5-phospho-D-arabinoyl)histamine
-
-
Ni2+

10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
phosphate

-
-
ribose 5-phosphate

-
1 mM, 12% inhibition
ribulose 5-phosphate

-
0.5 mM, 48% inhibition
sedoheptulose 7-phosphate

-
1 mM, 10% inhibition
sedoheptulose 7-phosphate
-
-
sorbitol-6-phosphate

-
-
suramin

-
no inhibition
suramin
an anti-trypanosomal drug
Zn2+

-
plastid enzyme is completely inhibited by 5 mM, activity of cytosolic isoenzyme is reduced to 49% of untreated control
Zn2+
10 mM, 89% inhibition, D-fructose 6-phosphate as substrate
additional information

analysis of genetic and structural basis for the development of fungal PGI inhibitors, docking study, overview
-
additional information
-
no inhibition by PCMB and iodoacetate
-
additional information
-
screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
-
additional information
N-substituted 5-phosphate-D-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: synthesis, structure-activity relationship and crystallographic studies, overview. N-substituted 5-phosphate-D-arabinonamide derivatives appear as strong PGI inhibitors
-
additional information
-
not inhibitory: EDTA
-
additional information
-
N-substituted 5-phosphate-D-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: synthesis, structure-activity relationship and crystallographic studies, overview. N-substituted 5-phosphate-D-arabinonamide derivatives appear as strong PGI inhibitors
-
additional information
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.1258 - 0.1778
alpha-D-glucose 6-phosphate
0.31 - 478
beta-D-fructose 6-phosphate
0.031 - 170
D-fructose 6-phosphate
1.029
D-galactose
-
pH 8.0, 40°C
0.084 - 267.4
D-glucose 6-phosphate
0.25 - 1.1
D-mannose 6-phosphate
0.01 - 0.74
fructose 6-phosphate
0.03 - 8
glucose 6-phosphate
133
L-talose
pH 7.0, 95°C
additional information
additional information
-
0.1258
alpha-D-glucose 6-phosphate

recombinant TaPGIp, pH 7.4, 22°C
0.1778
alpha-D-glucose 6-phosphate
recombinant TaPGIc, pH 7.4, 22°C
0.31
beta-D-fructose 6-phosphate

pH 7.0, 22°C, recombinant wild-type enzyme
233
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant H310A
376
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant Q415A
478
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant K422A
0.031
D-fructose 6-phosphate

pH 7.5, 30°C, recombinant mutant S278L
0.034
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
0.037
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.038
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
0.038
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
0.039
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
0.04
D-fructose 6-phosphate
-
50°C, pH 6.3
0.045
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
0.045
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
0.046
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
0.046
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
0.05
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
0.06
D-fructose 6-phosphate
-
pH 7.4, 80°C
0.061
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
0.063
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
0.063
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
0.068
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
0.14
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
0.1425
D-fructose 6-phosphate
-
-
0.147
D-fructose 6-phosphate
-
22°C, pH 7.4
0.18
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
0.19
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
0.2
D-fructose 6-phosphate
80°C, pH 7.4
0.21
D-fructose 6-phosphate
50°C, pH 7.4
0.22
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
0.23
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
0.25
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
0.27
D-fructose 6-phosphate
-
pH 7.6, 25°C
0.3
D-fructose 6-phosphate
-
pH 7.4, 50°C
0.318
D-fructose 6-phosphate
-
pH 7.6, 22°C
0.35
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
0.36
D-fructose 6-phosphate
-
pH 8.0
0.36
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.39
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
0.42
D-fructose 6-phosphate
50°C, pH 7.0, recombinant enzyme
0.44
D-fructose 6-phosphate
80°C, pH 7.4
0.46
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
0.5
D-fructose 6-phosphate
50°C
0.5
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
0.59
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme E89V
0.6
D-fructose 6-phosphate
-
pH 7.4, 50°C
0.6 - 3
D-fructose 6-phosphate
pH 7.0, 50°C
0.63
D-fructose 6-phosphate
50°C, pH 7.0, native enzyme
0.7
D-fructose 6-phosphate
-
pH 7.6, 37°C
0.8
D-fructose 6-phosphate
-
pH 7.4, 50°C
1
D-fructose 6-phosphate
-
80°C, pH 7.0, native enzyme
1.2
D-fructose 6-phosphate
-
80°C, pH 7.0, recombinant enzyme
1.4
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H137A
1.4
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
1.7
D-fructose 6-phosphate
50°C, pH 7.5, wild-type enzyme
2
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
2
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
2.1
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H91A
2.2
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
2.9
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
3
D-fructose 6-phosphate
-
pH 7.2, 37°C
3.5
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H89A
4
D-fructose 6-phosphate
-
80°C, pH not specified in the publication
20.3
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80A
169
D-fructose 6-phosphate
-
wild-type, 37°C, pH 8.0
170
D-fructose 6-phosphate
-
mutant A346H, 37°C, pH 8.0
0.084
D-glucose 6-phosphate

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.11
D-glucose 6-phosphate
-
ZR-82 cells, 22°C
0.18
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.2 - 1
D-glucose 6-phosphate
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.23
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.28
D-glucose 6-phosphate
-
22°C, pH 7.4
0.29
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.29
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.4
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.6
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.72
D-glucose 6-phosphate
80°C, pH 7.4
0.73
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.78
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.83
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
1
D-glucose 6-phosphate
-
50°C, pH 6.3
1
D-glucose 6-phosphate
-
pH 7.6, 37°C
1
D-glucose 6-phosphate
-
pH 7.2, 37°C
1.02
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.04
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.1
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
1.3
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
1.5
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
1.53
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.65
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1.86
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1.9
D-glucose 6-phosphate
-
pH 7.4, 80°C
1.9
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.99
D-glucose 6-phosphate
50°C, pH 7.0, native enzyme
1.99
D-glucose 6-phosphate
pH 7.0, 50°C
2
D-glucose 6-phosphate
50°C, pH 7.0, recombinant enzyme
2.11
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
2.43
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2.58
D-glucose 6-phosphate
-
mutant GroD1 cells, 22°C
2.7
D-glucose 6-phosphate
-
pH 7.4, 50°C
2.89
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
3.5
D-glucose 6-phosphate
80°C, pH 7.4
7.9
D-glucose 6-phosphate
-
80°C, pH 7.0, recombinant enzyme
8.7
D-glucose 6-phosphate
-
80°C, pH 7.0, native enzyme
11.7
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
221
D-glucose 6-phosphate
-
wild-type, 37°C, pH 8.0
267.4
D-glucose 6-phosphate
-
mutant A346H, 37°C, pH 8.0
0.25
D-mannose 6-phosphate

80°C, pH 7.4
1.1
D-mannose 6-phosphate
80°C, pH 7.4
0.01 - 0.17
fructose 6-phosphate

-
muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors
0.0186
fructose 6-phosphate
-
isomerase a
0.0205
fructose 6-phosphate
-
isomerase c
0.0213
fructose 6-phosphate
-
isomerase b
0.048
fructose 6-phosphate
-
-
0.0596
fructose 6-phosphate
-
mutant enzyme Thr224 to Met
0.0635
fructose 6-phosphate
-
native enzyme
0.0657
fructose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.07
fructose 6-phosphate
-
mammary gland enzyme
0.071
fructose 6-phosphate
-
-
0.0734
fructose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.0769
fructose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.09
fructose 6-phosphate
-
isozyme 1 and isozyme 2
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
fructose 6-phosphate, isozyme 4
0.1
fructose 6-phosphate
-
glucose 6-phosphate, soluble enzyme
0.11
fructose 6-phosphate
-
isozyme 3
0.11 - 0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
0.116
fructose 6-phosphate
-
-
0.119
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
fructose 6-phosphate, enzyme form PGI II
0.12
fructose 6-phosphate
-
fructose 6-phosphate, at pH 8.6
0.12
fructose 6-phosphate
-
glucose 6-phosphate
0.12
fructose 6-phosphate
-
liver enzyme
0.122
fructose 6-phosphate
-
-
0.167
fructose 6-phosphate
-
-
0.17
fructose 6-phosphate
-
enzyme form PGI I
0.18
fructose 6-phosphate
-
-
0.2
fructose 6-phosphate
-
glucose 6-phosphate, immobilized enzyme
0.2
fructose 6-phosphate
-
enzyme forms PGI I and PGI II
0.21
fructose 6-phosphate
-
erythrocyte enzyme, wild-type
0.228 - 0.278
fructose 6-phosphate
-
-
0.3
fructose 6-phosphate
-
isozyme 1 and 2
0.46
fructose 6-phosphate
-
glucose 6-phosphate, isozyme 2
0.48
fructose 6-phosphate
-
chloroplastic isoenzyme
0.74
fructose 6-phosphate
-
erythrocyte enzyme, mutant B9
0.03 - 0.8
glucose 6-phosphate

-
muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors
0.12 - 0.57
glucose 6-phosphate
-
mammary gland enzyme, values of 0.12 mM and 0.57 mM are determined by different authors
0.25
glucose 6-phosphate
-
-
0.27
glucose 6-phosphate
-
-
0.3 - 1.5
glucose 6-phosphate
-
values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors
0.351
glucose 6-phosphate
-
mutant enzyme Thr224 to Met
0.36
glucose 6-phosphate
-
-
0.44
glucose 6-phosphate
-
glucose 6-phosphate, enzyme form PGI I and PGI II
0.44
glucose 6-phosphate
-
glucose 6-phosphate
0.44
glucose 6-phosphate
-
at pH 8.6
0.445
glucose 6-phosphate
-
native enzyme
0.449
glucose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.45
glucose 6-phosphate
-
isozyme 4
0.505
glucose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.51
glucose 6-phosphate
-
isozyme 1
0.573
glucose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.58
glucose 6-phosphate
-
fructose 6-phosphate, cytosolic isoenzame
0.58
glucose 6-phosphate
-
isozyme 3
0.6
glucose 6-phosphate
-
liver enzyme
2
glucose 6-phosphate
-
-
2
glucose 6-phosphate
-
-
5.9
glucose 6-phosphate
-
isozyme 2
8
glucose 6-phosphate
-
glucose 6-phosphate, cytosolic and chloroplastic isoenzyme
8
glucose 6-phosphate
-
isozyme 1
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
the pH-value has a great influence on the Km-value for fructose 6-phosphate
-
additional information
additional information
kinetics for aldose substrates, overview
-
additional information
additional information
-
kinetics for aldose substrates, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetic analysis, recombinant enzyme
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
124 - 1275
alpha-D-glucose 6-phosphate
17.4 - 86
beta-D-fructose 6-phosphate
0.0003 - 650
D-fructose 6-phosphate
0.04 - 2765
D-glucose 6-phosphate
3330
fructose 6-phosphate
-
isomerase a
475.5
L-talose
pH 7.0, 95°C
124
alpha-D-glucose 6-phosphate

recombinant TaPGIp, pH 7.4, 22°C
1275
alpha-D-glucose 6-phosphate
recombinant TaPGIc, pH 7.4, 22°C
17.4
beta-D-fructose 6-phosphate

pH 7.0, 22°C, recombinant wild-type enzyme
65
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant H310A
70
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant Q415A
86
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant K422A
0.0003
D-fructose 6-phosphate

50°C, pH 7.5, mutant enzyme E98V
0.021
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H89A
0.06
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
0.07
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
0.22
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.32
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
0.34
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H137A
0.42
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
0.43
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80A
0.5
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H91A
0.6
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant S278L
0.68
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
1.9
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
5
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
8.4
D-fructose 6-phosphate
50°C
11.6
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
15
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
18
D-fructose 6-phosphate
-
pH 8.0
19
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
26
D-fructose 6-phosphate
50°C, pH 7.5, wild-type enzyme
30.8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
32.4
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
42
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
75
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
76
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
93
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
100
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
150
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
160
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
190
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
190
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
300
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
420
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
650
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.04
D-glucose 6-phosphate

kcat below 0.04 s-1mutant enzyme H389L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.04
D-glucose 6-phosphate
kcat below 0.04 s-1,mutant enzyme K362A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant S278L
0.6
D-glucose 6-phosphate
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.3
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.6
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
4 - 5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
17
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
21
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
31
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
42
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
61
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
63
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
80
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
110
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
120
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
130
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
140
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
240
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
260
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
340
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
350
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
360
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
380
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
470
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
470
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
500
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
729
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
750
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
929
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
946
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1000
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
1091
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
2009
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2198
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2433
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2765
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
985.7 - 7171
alpha-D-glucose 6-phosphate
0.18 - 56.13
beta-D-fructose 6-phosphate
0.02 - 162
D-fructose 6-phosphate
2.7 - 1700
D-glucose 6-phosphate
3.58
L-talose
pH 7.0, 95°C
985.7
alpha-D-glucose 6-phosphate

recombinant TaPGIp, pH 7.4, 22°C
7171
alpha-D-glucose 6-phosphate
recombinant TaPGIc, pH 7.4, 22°C
0.18
beta-D-fructose 6-phosphate

pH 7.0, 22°C, recombinant mutant K422A
0.19
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant Q415A
0.28
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant mutant H310A
56.13
beta-D-fructose 6-phosphate
pH 7.0, 22°C, recombinant wild-type enzyme
0.02
D-fructose 6-phosphate

pH 7.4, 70°C, mutant enzyme H80A
0.02
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
0.035
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
0.61
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.64
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
1.1
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
2.27
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
3.8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
4
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
8.3
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
8.6
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
11.5
D-fructose 6-phosphate
pH 7.0, 50°C, native enzyme
16.5
D-fructose 6-phosphate
pH 7.0, 50°C, recombinant enzyme
130
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
162
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
2.7
D-glucose 6-phosphate

mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
6.2
D-glucose 6-phosphate
pH 7.0, 50°C, native enzyme
6.7
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
7.4
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
8.5
D-glucose 6-phosphate
pH 7.0, 50°C, recombinant enzyme
72
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
90
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
450
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
489
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
490
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
517
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
610
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
618
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
715
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
790
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
906
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
957
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1100
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
1218
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1308
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1700
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
-
high polymorphism in PGI is common in insects, and an association between thermal adaptation and PGI variations are observed in some insects. 5 Alleles are found in the Finnish population, with pgi-d1 being the most common allele, while 2 alleles are found in the Chinese population, with the newly discovered pgig3 allele as the most common, sequence comparisons. Identification of 3 amino acid substitutions in phosphoglucose isomerase (PGI) that are related to thermostability in the Glanville fritillary butterfly (Melitaea cinxia). Comparison of enzyme properties of enzyme from different populations, overview
malfunction

deficiency of the enzymatic activity in red blood cells causes nonspherocytic hemolytic anemia
malfunction
-
PGI/AMF is correlated with breast cancer and poor prognosis in breast cancer. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
malfunction
-
neuromuscular symptoms are associated with inherited GPI deficiency
malfunction
enzyme deficiency leads to nonspherocytic hemolytic anemia
malfunction
-
hyphal growth, conidial germination, and septa formation are significantly inhibited in FgGPI deletion mutant DELTAFgGPI. In addition, pyruvate production, deoxynivalenol (DON) biosynthesis, and virulence are reduced in DELTAFgGPI. Carbendazim-resistant substitutions in beta2 tubulin reduce the interaction intensity between FgGPI and Fgbeta2, thereby increasing FgGPI expression and accelerating DON biosynthesis in carbendazim-resistant strains
malfunction
the growth of Aspergillus fumigatus is repressed by the deletion of pgi, which can be rescued by glucose and fructose supplementation in a 1:10 ratio. Even under these optimized growth conditions, the DELTApgi mutant exhibits severe cell wall defects, retarded development, and attenuated virulence in Caenorhabditis elegans and Galleria mellonella infection models. The pgi deletion affects homeostasis of intracellular nucleotide sugars and phosphate sugars. Gene pgi deletion leads to attenuated virulence in nematode (Caenorhabditis elegans) and larva infection models, overview
malfunction
the loss of PGI1 impairs the conversion of F6P of the Calvin-Benson cycle to G6P for the synthesis of transitory starch in leaf chloroplasts. Loss of PGI1 impairs the conversion of F6P of the Calvin-Benson cycle to glucose 6-phosphate (G6P) for the synthesis of transitory starch in leaf chloroplasts. Since cpgi knockout mutants have not yet been obtained, they are thought to be lethal. The cpgi lethality can be rescued by expressing CaMV 35S promoter (p35S)-driven cPGI. But the complemented line is completely sterile due to pollen degeneration. A cpgi mutant expressing p35S::cPGI-YFP, in which YFP fluorescence in developing anthers, is undetectable specifically in the tapetum and in pollen, which can be associated with male sterility. RNAi-cPGI knockdown lines with strong cPGI repression in floral buds are generated that exhibit reduced male fertility due to the degeneration of most pollen. Histological analyses indicate that the synthesis of intersporal callose walls is impaired, causing microsporocytes to fail to separate haploid daughter nuclei to form tetrads, which might be responsible for subsequent pollen degeneration. cpgi knockout mutantsare isolated in the progeny of a heterozygous cpgi mutant floral-dipped with sugar solutions. The rescued cpgi mutants exhibit diminished young vegetative growth, reduced female fertility, and impaired intersporal callose wall formation in a meiocyte, and, thus, male sterility. The cpgi-3 knockout mutation likely impairs pre-globular embryo development. Phenotypic analysis of homozygous cpgi mutants. Phenotypes, overview
malfunction
the TmPGI E281A/Q415A and H310A/K422A double mutations show abolished activity, suggesting that there are redundant catalytic residues, and Q415 may participate in sugar phosphate isomerization upon E281 mutation. The catalytic role of E281 can be compensated by other residues such as Q415. Activity assays additionally show that H310, Q415, and K422 mutations reduce activity yet none of the mutations abolish activity, only E281A/ Q415A and H310A/K422A double mutations are inactive
malfunction
gene lepgi-silenced strains have significantly less biomass than the wild-type strain. Furthermore, the extracellular polysaccharide (EPS) and intracellular polysaccharide (IPS) levels increase 1.5 to 3fold and 1.5fold, respectively, in lepgi-silenced strains. The cell wall integrity in the silenced strains is also altered, which might be due to changes in the compounds and structure of the cell wall. The results show that compared to wild-type, silencing gene lepgi leads to a significant decrease of approximately 40% in the beta-1,3-glucan content, and a significant increase of 2-3fold in the chitin content. Altered cell wall composition, overview
malfunction
-
the TmPGI E281A/Q415A and H310A/K422A double mutations show abolished activity, suggesting that there are redundant catalytic residues, and Q415 may participate in sugar phosphate isomerization upon E281 mutation. The catalytic role of E281 can be compensated by other residues such as Q415. Activity assays additionally show that H310, Q415, and K422 mutations reduce activity yet none of the mutations abolish activity, only E281A/ Q415A and H310A/K422A double mutations are inactive
-
malfunction
-
the growth of Aspergillus fumigatus is repressed by the deletion of pgi, which can be rescued by glucose and fructose supplementation in a 1:10 ratio. Even under these optimized growth conditions, the DELTApgi mutant exhibits severe cell wall defects, retarded development, and attenuated virulence in Caenorhabditis elegans and Galleria mellonella infection models. The pgi deletion affects homeostasis of intracellular nucleotide sugars and phosphate sugars. Gene pgi deletion leads to attenuated virulence in nematode (Caenorhabditis elegans) and larva infection models, overview
-
malfunction
-
the TmPGI E281A/Q415A and H310A/K422A double mutations show abolished activity, suggesting that there are redundant catalytic residues, and Q415 may participate in sugar phosphate isomerization upon E281 mutation. The catalytic role of E281 can be compensated by other residues such as Q415. Activity assays additionally show that H310, Q415, and K422 mutations reduce activity yet none of the mutations abolish activity, only E281A/ Q415A and H310A/K422A double mutations are inactive
-
malfunction
-
the TmPGI E281A/Q415A and H310A/K422A double mutations show abolished activity, suggesting that there are redundant catalytic residues, and Q415 may participate in sugar phosphate isomerization upon E281 mutation. The catalytic role of E281 can be compensated by other residues such as Q415. Activity assays additionally show that H310, Q415, and K422 mutations reduce activity yet none of the mutations abolish activity, only E281A/ Q415A and H310A/K422A double mutations are inactive
-
malfunction
-
the TmPGI E281A/Q415A and H310A/K422A double mutations show abolished activity, suggesting that there are redundant catalytic residues, and Q415 may participate in sugar phosphate isomerization upon E281 mutation. The catalytic role of E281 can be compensated by other residues such as Q415. Activity assays additionally show that H310, Q415, and K422 mutations reduce activity yet none of the mutations abolish activity, only E281A/ Q415A and H310A/K422A double mutations are inactive
-
malfunction
-
gene lepgi-silenced strains have significantly less biomass than the wild-type strain. Furthermore, the extracellular polysaccharide (EPS) and intracellular polysaccharide (IPS) levels increase 1.5 to 3fold and 1.5fold, respectively, in lepgi-silenced strains. The cell wall integrity in the silenced strains is also altered, which might be due to changes in the compounds and structure of the cell wall. The results show that compared to wild-type, silencing gene lepgi leads to a significant decrease of approximately 40% in the beta-1,3-glucan content, and a significant increase of 2-3fold in the chitin content. Altered cell wall composition, overview
-
malfunction
-
hyphal growth, conidial germination, and septa formation are significantly inhibited in FgGPI deletion mutant DELTAFgGPI. In addition, pyruvate production, deoxynivalenol (DON) biosynthesis, and virulence are reduced in DELTAFgGPI. Carbendazim-resistant substitutions in beta2 tubulin reduce the interaction intensity between FgGPI and Fgbeta2, thereby increasing FgGPI expression and accelerating DON biosynthesis in carbendazim-resistant strains
-
metabolism

PGI is the second enzyme of glycolysis
metabolism
-
PGI is the second enzyme of glycolysis
metabolism
-
PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
metabolism
-
key enzyme in the AMF signaling pathway, overview
metabolism
GPI plays an important role in glycolysis
metabolism
-
phosphoglucose isomerase is a key enzyme in the glycolysis and glycogenesis pathways
metabolism
PGI is involved in glycolysis and the pentose phosphate pathway (PPP)
metabolism
-
PGI catalyzes the second step of glycolysis, a central metabolic process that occurs in all living organisms
metabolism
-
GPI plays an important role in glycolysis
-
metabolism
-
PGI is the second enzyme of glycolysis
-
metabolism
-
PGI is involved in glycolysis and the pentose phosphate pathway (PPP)
-
physiological function

-
PGI/AMF is a housekeeping gene product/cytokine that catalyzes a step in glycolysis and gluconeogenesis, and acts as a multifunctional cytokine associated with aggessive tumors. PGI/AMF induces a mesenchymal-like morphologic conversion being a key enzyme for both epithelial-to-mesenchymal transition in the initiating step of cancer metastasis and mesenchymal-to-epithelial transition in the late stage of metastasis during breast cancer progression, overview
physiological function
-
multifunctional protein GPI is an endogenous inhibitor to myofibril-bound serine proteinase, and may play a significant role in the regulation of muscular protein metabolism in vivo
physiological function
-
AMF is critical for the migration, invasion, metastasis, and anti-apoptotic effects of malignant tumor cells, and its multiple roles in tumor progression may be mediated by certain downstream pathways and effectors. Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8, overview
physiological function
-
the Pgi activity is limiting in the control BL310 strain during growth on lactose or galactose. The level of Pgi enzyme activity controls the level of production of those UDP-glucose and UDP-galactose in galactose
physiological function
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
autocrine motility factor/phosphoglucose isomerase (AMF/PGI) regulates endoplasmic reticulm (ER) stress and cell death through control of ER calcium release. AMF/PGI also protects against thapsigargin- and tunicamycin-induced ER stress and apoptosis and suppresses cytosolic Ca2+ homeostasis
physiological function
the enzyme is part of the Pyrococcus furiosus variant of the Embden-Meyerhof pathway
physiological function
-
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose
physiological function
starch content in leaves completely lacking PGI1 activity is about 10-15% of that of wild type leaves and can be be reverted by the introduction of a sex1 null mutation impeding beta-amylolytic starch breakdown. In mutant strains, starch granules are present in the chloroplasts of mesophyll cells and plastidic and extra-plastidic beta-amylase encoding genes are higly expressed in leaves. Mutant strains display slow growth and reduced photosynthetic capacity phenotypes even under continuous light conditions
physiological function
-
glucose-6-phosphate isomerase FgGPI, a beta2 tubulin-interacting protein, is indispensable for fungal development and deoxynivalenol biosynthesis in Fusarium graminearum, for glucose metabolism and common carbon source utilization. The enzyme is also positively associated with glucose metabolism, ATP biosynthesis, and carbon source utilization. FgGPI interacts with Fgbeta2. Indispensable role of FgGPI in fungal developmental processes, DON biosynthesis, and pathogenicity in Fusarium graminearum
physiological function
phosphoglucose isomerase (PGI) is a glycolytic enzyme that catalyzes the reversible conversion of glucose-6-phosphate (Glc6P) to fructose-6-phosphate (Fru6P), a key precursor of fungal cell wall biosynthesis. Therefore, PGI is involved in glycolysis and the pentose phosphate pathway (PPP). PGI is required for Aspergillus fumigatus survival and maintenance of metabolic homeostasis. AfPGI plays a key role in maintaining the level of intracellular nucleotide sugars (UDP-Glc, UDP-GlcNAc, and GDP-Man) in Aspergillus fumigatus. AfPGI is a key enzyme in maintaining the homeostasis of intracellular phosphate sugars
physiological function
cytosolic PGI (PGIc) is involved in sucrose synthesis and glycolysis. During the day, triose phosphates from photosynthesis are exported to the cytosol and converted to fructose 6-phosphate (F6P) which is converted to glucose 6-phosphate (G6P) catalyzed by PGIc. Both hexose phosphate are substrates in sucrose synthesis. The concentration of G6P is greater in the cytosol than the chloroplast stroma both day and night
physiological function
phosphoglucose isomerase (PGI) catalyzes the interconversion of fructose-6-phosphate and glucose-6-phosphate, which impacts cell carbon metabolic flow. Arabidopsis (Arabidopsis thaliana) contains two nuclear PGI genes respectively encoding plastidial PGI1 and cytosolic PGI (cPGI). Cytosolic phosphoglucose isomerase (cPGI) plays a vital role in carbohydrate partitioning, which is indispensable for microsporogenesis and early embryogenesis. cPGI is required for normal male fertility, role of cPGI in pollen development
physiological function
phosphoglucose isomerases (PGIs) belong to a class of enzymes that catalyze the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGIs are crucial in glycolysis and gluconeogenesis pathways and proposed as serving additional extracellular functions in eukaryotic organisms
physiological function
phosphoglucose isomerase (PGI) is a cytosolic enzyme that catalyzes the reversible interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate in glycolysis. Outside the cell, PGI is also known as autocrine motility factor (AMF), a cytokine secreted by a large variety of tumor cells that stimulates motility of cancer cells in vitro and metastases development in vivo
physiological function
-
phosphoglucose isomerase (PGI) is a cytosolic enzyme that catalyzes the reversible interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate in glycolysis
physiological function
-
glucose-6-phosphate isomerase (G6PI) catalyses the second step in glycolysis in the reversible interconversion of an aldohexose glucose 6-phosphate, a six membered ring moiety to a ketohexose, fructose 6-phosphate five membered ring moiety. This enzyme is of utmost importance due to its multifunctional role like neuroleukin, autocrine motility factor and others in various species
physiological function
phosphoglucose isomerase (PGI) is a key enzyme that participates in polysaccharide synthesis, which is responsible for the interconversion of glucose-6-phosphate (G-6-P) and fructose-6-phosphate (F6-P). Roles of pgi in hyphal growth, polysaccharide synthesis, and cell wall integrity, overview. The lepgi gene positively regulates the growth, while pgi has a negative regulatory effect on polysaccharide synthesis, including both EPS and IPS. Cell wall integrity of the silenced strains change and lepgi participates in the process that regulates cell wall integrity
physiological function
the dianionic phosphate group (DPG) is an essential fragment of signaling biological molecules and protein-binding ligands. It is a constitutive fragment of biosensors, which binds to the dimer interface of phosphoglucose isomerase (PGI), an intracellular enzyme involved in sugar metabolism, as well as an extracellular protein known as autocrine motility factor (AMF) closely related to metastasis formation. PGI reversibly isomerizes glucose 6-phosphate into fructose-6-phosphate (F6P) in glycolysis. Outside the cell, it acts as the cytokine autocrine motility factor (AMF), a cancer progression biomarker
physiological function
-
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
-
physiological function
-
phosphoglucose isomerases (PGIs) belong to a class of enzymes that catalyze the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGIs are crucial in glycolysis and gluconeogenesis pathways and proposed as serving additional extracellular functions in eukaryotic organisms
-
physiological function
-
phosphoglucose isomerase (PGI) is a glycolytic enzyme that catalyzes the reversible conversion of glucose-6-phosphate (Glc6P) to fructose-6-phosphate (Fru6P), a key precursor of fungal cell wall biosynthesis. Therefore, PGI is involved in glycolysis and the pentose phosphate pathway (PPP). PGI is required for Aspergillus fumigatus survival and maintenance of metabolic homeostasis. AfPGI plays a key role in maintaining the level of intracellular nucleotide sugars (UDP-Glc, UDP-GlcNAc, and GDP-Man) in Aspergillus fumigatus. AfPGI is a key enzyme in maintaining the homeostasis of intracellular phosphate sugars
-
physiological function
-
phosphoglucose isomerases (PGIs) belong to a class of enzymes that catalyze the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGIs are crucial in glycolysis and gluconeogenesis pathways and proposed as serving additional extracellular functions in eukaryotic organisms
-
physiological function
-
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose
-
physiological function
-
phosphoglucose isomerases (PGIs) belong to a class of enzymes that catalyze the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGIs are crucial in glycolysis and gluconeogenesis pathways and proposed as serving additional extracellular functions in eukaryotic organisms
-
physiological function
-
phosphoglucose isomerases (PGIs) belong to a class of enzymes that catalyze the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. PGIs are crucial in glycolysis and gluconeogenesis pathways and proposed as serving additional extracellular functions in eukaryotic organisms
-
physiological function
-
phosphoglucose isomerase (PGI) is a key enzyme that participates in polysaccharide synthesis, which is responsible for the interconversion of glucose-6-phosphate (G-6-P) and fructose-6-phosphate (F6-P). Roles of pgi in hyphal growth, polysaccharide synthesis, and cell wall integrity, overview. The lepgi gene positively regulates the growth, while pgi has a negative regulatory effect on polysaccharide synthesis, including both EPS and IPS. Cell wall integrity of the silenced strains change and lepgi participates in the process that regulates cell wall integrity
-
physiological function
-
glucose-6-phosphate isomerase FgGPI, a beta2 tubulin-interacting protein, is indispensable for fungal development and deoxynivalenol biosynthesis in Fusarium graminearum, for glucose metabolism and common carbon source utilization. The enzyme is also positively associated with glucose metabolism, ATP biosynthesis, and carbon source utilization. FgGPI interacts with Fgbeta2. Indispensable role of FgGPI in fungal developmental processes, DON biosynthesis, and pathogenicity in Fusarium graminearum
-
additional information

the phosphate recognition site is a loop consisting of Ser215, Lys216, Thr217, and Thr220. Ser165 also forms a hydrogen bond with the phosphate group. Hydroxyl groups on the sugar ring form hydrogen bonds to Gly164, Glu363, His394, and Lys516. Sequence alignment shows that these residues are conserved in all PGI orthologues and contribute to a conserved reaction mechanism
additional information
comparison between apo and G6P binding PGIc structures reveals that substrate binding induces a position shift of amino acids in the binding pocket, resulting in tight binding of the substrate. The binding pocket in plastidic TaPGIp is different from that in TaPGIc, though they are constituted by the same conserved amino acids. The G6P binding pocket of isozyme PGIc is formed with Gly156, Ser157, Ser212, Lys213, Thr214, Thr217, Gln356 from one subunits and His391 from the other subunit
additional information
comparison between apo and G6P binding PGIc structures reveals that substrate binding induces a position shift of amino acids in the binding pocket, resulting in tight binding of the substrate. The binding pocket in plastidic TaPGIp is different from that in TaPGIc, though they are constituted by the same conserved amino acids
additional information
PGI crystal structure analysis and computational docking, structure-function analysis, structure comparisons, overview. TmPGI E281 participates directly in the cis-enediol intermediate step, and either H310 or K422 may facilitate sugar ring opening and closure. Residues are conserved active site residues E281, H310, Q415, and K422. Residue E281 is most important for TmPGI formation of the cis-enediol intermediate, and the presence of either H310 or K422 is required for catalysis, similar to previous observations from homologous PGIs. E281 is important but not essential for TmPGI activity
additional information
-
enzyme structure homology modeling, the structure is superposed with human enzyme structure, PDB ID 1IAT_A, and ligand structure, PDB ID 1U0G_A
additional information
-
molecular modeling and molecular dynamics simulation of PGI, three-dimensional enzyme structure, detailed overview
additional information
dianionic phosphate group (DPG) presentation in molecular mechanics, overview. Design of DPG-based biosensors with enhanced affinities for AMF/PGI cancer biomarker in blood. Ab initio computed (SIBFA) polarizable molecular dynamics and ab initio quantum chemistry (QC) calculations. Analysis of bi-molecular complexes of DPG with the main-chain and side-chain PGI residues, which bind to it in the recognition site, DPG and the His389 side chain, close to Thr215 and Lys519 for DPG, and to Glu217 for His389
additional information
-
Bdellovibrio bacteriovorus phosphoglucose isomerase structures reveal rigidity in the active site of a selected subset of enzymes upon substrate binding. An induced-fit conformational change within the active site is not a prerequisite for the binding of substrates in some PGIs. A phenylalanine residue, conserved across most PGI enzymes but substituted for glycine Bdellovibrio bacteriovorus and other select organisms, is central to the induced-fit mode of substrate recognition for PGIs. The Bdellovibrio bacteriovorus PGI represents the smallest conventional PGI characterized to date and probably represents the minimal requirements for a functional PGI. The BbPGI active site, in contrast to those of previously characterized PGIs, does not undergo significant conformational change upon substrate binding. This lack of active site mobility can be partially attributed to the substitution of a Phe residue, conserved in most PGIs, for a Gly residue in BbPGI. We also note a distinct feature in the smaller PGIs wherein the hook region is in a different position to that of the larger PGI structures
additional information
-
PGI crystal structure analysis and computational docking, structure-function analysis, structure comparisons, overview. TmPGI E281 participates directly in the cis-enediol intermediate step, and either H310 or K422 may facilitate sugar ring opening and closure. Residues are conserved active site residues E281, H310, Q415, and K422. Residue E281 is most important for TmPGI formation of the cis-enediol intermediate, and the presence of either H310 or K422 is required for catalysis, similar to previous observations from homologous PGIs. E281 is important but not essential for TmPGI activity
-
additional information
-
the phosphate recognition site is a loop consisting of Ser215, Lys216, Thr217, and Thr220. Ser165 also forms a hydrogen bond with the phosphate group. Hydroxyl groups on the sugar ring form hydrogen bonds to Gly164, Glu363, His394, and Lys516. Sequence alignment shows that these residues are conserved in all PGI orthologues and contribute to a conserved reaction mechanism
-
additional information
-
PGI crystal structure analysis and computational docking, structure-function analysis, structure comparisons, overview. TmPGI E281 participates directly in the cis-enediol intermediate step, and either H310 or K422 may facilitate sugar ring opening and closure. Residues are conserved active site residues E281, H310, Q415, and K422. Residue E281 is most important for TmPGI formation of the cis-enediol intermediate, and the presence of either H310 or K422 is required for catalysis, similar to previous observations from homologous PGIs. E281 is important but not essential for TmPGI activity
-
additional information
-
PGI crystal structure analysis and computational docking, structure-function analysis, structure comparisons, overview. TmPGI E281 participates directly in the cis-enediol intermediate step, and either H310 or K422 may facilitate sugar ring opening and closure. Residues are conserved active site residues E281, H310, Q415, and K422. Residue E281 is most important for TmPGI formation of the cis-enediol intermediate, and the presence of either H310 or K422 is required for catalysis, similar to previous observations from homologous PGIs. E281 is important but not essential for TmPGI activity
-
additional information
-
PGI crystal structure analysis and computational docking, structure-function analysis, structure comparisons, overview. TmPGI E281 participates directly in the cis-enediol intermediate step, and either H310 or K422 may facilitate sugar ring opening and closure. Residues are conserved active site residues E281, H310, Q415, and K422. Residue E281 is most important for TmPGI formation of the cis-enediol intermediate, and the presence of either H310 or K422 is required for catalysis, similar to previous observations from homologous PGIs. E281 is important but not essential for TmPGI activity
-
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118000
-
isoenzymes 1-4, gel filtration
120000 - 127000
Cassia coluteoides
-
gel filtration, density gradient centrifugation
120000 - 130000
-
low-molecular weight form PGI I, gel filtration, sucrose density gradient centrifugation
135000
-
enzyme form A, gel filtration
145000
-
calculation from sedimentation coefficient and diffusion coefficient
172000
-
sedimentation equilibrium analysis
202000 - 204000
-
gel filtration, electrophoresis of the enzyme cross-linked with dimethyl adipimidate
21500
x * 21476, sequence calculation, x * 21500, SDS-PAGE
220000 - 234000
-
high-molecular weight form PGI II, gel filtration
23500
2 * 23500, SDS-PAGE
24000
-
x * 24000, SDS-PAGE
24675
-
x * 24675, calculated from amino acid sequence
26834
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
27424
-
1 * 27424, calculated, 1 * 28000, SDS-PAGE
30209
-
1 * 30209, calculated, 1 * 28000, SDS-PAGE
32000
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
33548
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
34684
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
35000
2 * 35000, SDS-PAGE, 2 * 35150, calculated
35150
2 * 35000, SDS-PAGE, 2 * 35150, calculated
36100
2 * 36000, SDS-PAGE, 2 * 36100, calculated
41000
-
native enzyme, gel filtration
49000
-
x * 49000, free enzyme, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
50600
-
4 * 50600, SDS-PAGE
56000
-
x * 56000, enzyme variant C, SDS-PAGE
57000
-
x * 57000, enzyme variant B, SDS-PAGE
61310
-
x * 61310, calculation from nucleotide sequence
61450
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
63000
-
2 * 63000, sedimentation velocity ultracentrifugation of enzyme dissociated in 6 M guanidine/HCl
6320
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
63200
-
2 * 63200, A-type subunit, isoenzyme 1 and 2, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
67113
-
x * 67113, calculation from nucleotide sequence
67700
-
enzyme form B, gel filtration
70700
-
2 * 70700, isomerase A, SDS-PAGE
73300
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
75000
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
110000

-
sedimentation equilibrium analysis
120000

-
-
120000
-
isoenzyme A, B and C, sedimentation equilibrium ultracentrifugation, gel electrophoresis
120000
-
gel filtration, sucrose density gradient centrifugation
120000
-
isoenzyme 1 and 2, sedimentation velocity centrifugation
125000

-
cytosolic isoenzyme, gel filtration
125000
-
cytosolic isoenzyme, gel filtration
125000
-
cytosolic isoenzyme, gel filtration
125000
-
isomerase a, sedimentation equilibrium analysis
132000

-
high speed equilibrium sedimentation
132000
-
sedimentation velocity ultracentrifugation
140000

-
plastidic isoenzyme, gel filtration
140000
-
plastidic isoenzyme, gel filtration
140000
-
plastidic isoenzyme, gel filtration
21476

x * 21476, sequence calculation, x * 21500, SDS-PAGE
21476
2 * 21476, calculated from sequence
23000

-
2 * 23000, SDS-PAGE
23000
2 * 23000, SDS-PAGE
27000

-
analytical ultracentrifugation
27000
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
28000

-
gel filtration
34000

-
2 * 34000, enzyme form B, gel filtration after equilibration with SDS
34000
-
4 * 34000, enzyme form A, gel filtration after equilibration with SDS
36000

-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
36000
2 * 36000, SDS-PAGE, 2 * 36100, calculated
45000

gel filtration
45000
-
2 * 45000, SDS-PAGE
48000

-
mammary gland, low speed sedimentation without reaching equilibrium
55000

-
x * 55000
55000
-
1 * 55000 + 1 * 65000, SDS-PAGE
59000

-
2 * 59000, isoenzyme 1-5, SDS-PAGE
59000
-
2 * 59000, low-molecular weight form, SDS-PAGE
59000
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
60000

-
x * 60000, enzyme variant A, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE, gel filtration in 6 M guanidine-HCl
61000

-
2 * 61000, SDS-PAGE
61000
-
2 * 61000, SDS-PAGE
61000
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
65000

-
sedimentation equilibrium, analytical ultracentrifugation
65000
-
x * 65000, recombinant enzyme, SDS-PAGE
65000
-
1 * 55000 + 1 * 65000, SDS-PAGE
67000

-
gel filtration
67000
analytical ultracentrifugation
69800

-
2 * 69800, B-type subunit, isoenzyme 4, SDS-PAGE
69800
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
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heterodimer
-
1 * 55000 + 1 * 65000, SDS-PAGE
?

-
x * 49000, free enzyme, SDS-PAGE
?
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
?
-
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
-
?
-
x * 56000, enzyme variant C, SDS-PAGE
?
-
x * 60000, enzyme variant A, SDS-PAGE
?
-
x * 57000, enzyme variant B, SDS-PAGE
?
-
x * 67113, calculation from nucleotide sequence
?
-
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 61000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 21476, sequence calculation, x * 21500, SDS-PAGE
?
-
x * 61310, calculation from nucleotide sequence
?
-
x * 24675, calculated from amino acid sequence
dimer

2 * 36000, SDS-PAGE, 2 * 36100, calculated
dimer
-
2 * 59000, isoenzyme 1-5, SDS-PAGE
dimer
-
2 * 59000, low-molecular weight form, SDS-PAGE
dimer
-
2 * 59000, low-molecular weight form, SDS-PAGE
-
dimer
-
2 * 70700, isomerase A, SDS-PAGE
dimer
-
2 * 69800, B-type subunit, isoenzyme 4, SDS-PAGE
dimer
-
2 * 63000, sedimentation velocity ultracentrifugation of enzyme dissociated in 6 M guanidine/HCl
dimer
-
2 * 63200, A-type subunit, isoenzyme 1 and 2, SDS-PAGE
dimer
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
dimer
-
2 * 34000, enzyme form B, gel filtration after equilibration with SDS
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
dimer
-
2 * 60000-70000, SDS-PAGE, SDS velocity centrifugation, maleic anhydride velocity and equilibrium sedimentation, urea velocity sedimentation, propionic acid velocity sedimentation guanidine-HCl velocity and equilibrium sedimentation
dimer
the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit
dimer
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
dimer
2 * 23000, SDS-PAGE
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE, gel filtration in 6 M guanidine-HCl
dimer
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
dimer
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 63000-67000, SDS-PAGE, analytical ultracentrifugation in 6 M guanidine/HCl
dimer
2 * 35000, SDS-PAGE, 2 * 35150, calculated
dimer
structure and active site conformation, overview
dimer
-
structure and active site conformation, overview
-
dimer
-
2 * 60000-67000, SDS-PAGE
homodimer

2 * 61700, about, isozyme PGIc, sequence calculation, 2 * 90000, about, recombinant cPGI-YFP fusion protein, SDS-PAGE
homodimer
the structure of the AfPGI monomer in the asymmetric unit contains a large domain and a small domain. Each domain exhibits an alpha/beta fold in which a central beta-sheet is flanked by alpha-helixes
homodimer
-
the structure of the AfPGI monomer in the asymmetric unit contains a large domain and a small domain. Each domain exhibits an alpha/beta fold in which a central beta-sheet is flanked by alpha-helixes
-
homodimer
x-ray crystallography
homodimer
-
x-ray crystallography
-
homodimer
2 * 23500, SDS-PAGE
homodimer
2 * 21476, calculated from sequence
homodimer
both recombinantly purified cytosolic TaPGIc and plastidic TaPGIp proteins are mainly homodimeric. Both PGIc and PGIp are dimeric but with different shapes: PGIc appears like a ball and PGIp looks like a diamond. Compared to PGIp, the compaction in PGIc is tighter with more contact amino acids between its two subunits resulting in a larger interface area, which might account for its higher thermal stability. The electrostatic surface is more positive in PGIc than in PGIp. For both proteins, the residues at the interface between two subunits are more conserved than those on the surface. Structural comparison and sequence alignment between TaPGIc and TaPGIp monomer. The last helix is essential for dimer formation and the dimer is the functional unit for PGIs
monomer

-
1 * 27424, calculated, 1 * 28000, SDS-PAGE
monomer
-
1 * 30209, calculated, 1 * 28000, SDS-PAGE
tetramer

-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
tetramer
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
-
tetramer
-
4 * 34000, enzyme form A, gel filtration after equilibration with SDS
tetramer
-
4 * 50600, SDS-PAGE
additional information

-
in BbPGI and PGIs of less than 450 aa, an alternative conformation is adopted with an extension of the loop from the N-terminus of alpha20. BbPGI is composed of three domains: the large domain, consisting of residues 1-31 and 213-384 which forms a mixed 5-strand beta-sheet sandwiched by alpha-helices, and the small domain, consisting of residues 44-195 which forms a parallel 5-strand beta-sheet flanked by alpha-helices and the C-terminal arm subdomain, a single alpha-helix composed of residues 392-408. The small and large domains are linked to each other by residues 32-43 and 196-212, with residues 199-211 forming an alpha-helix. A small loop (residues 385-391) connects the large domain to the C-terminal arm subdomain. A hook region (residues 306-348) extends from the large domain and packs against the small domain of the dimer partner providing dimer-stabilizing hydrogen bonding and hydrophobic interactions. Positioning of the hook region varies in PGIs, with the interaction loop extending from either the N-terminus or C-terminus of alpha20 (BbPGI helix numbering) to interact with either the small domain or large domain of the dimer partner, respectively. All three domains contribute to the proposed active site, with the small domain positioned to coordinate the phosphoryl group of the incoming substrate. Active site architecture is completed by recruitment of the large domain of a dimer partner. This is necessary for catalysis since the dimer partner donates the conserved residue H285 required for sugar ring-opening/closing. BbPGI active site and ligand accommodation/coordination, dimer formation, detailed overview
additional information
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
additional information
-
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
additional information
-
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
-
additional information
structure homology modelling, overview
additional information
-
structure homology modelling, overview
additional information
-
interaction of enzyme with insulin-like growth factor binding protein-3, both glycosylated and unglycosylated, results in formation of a complex of 80 kDa and in dose-dependent inhibition of enzyme
additional information
-
poly(AFP-ribose)polymerase-14, i.e. PARP-14, is a binding partner of phosphoglucose isomerase/autocrine motility factor. Phosphoglucose isomerase/autocrine motility factor is degraded via the ubiquitin-lysosome system, and PARP-14 inhibits the ubiquitination of the enzyme thus contributing to its stabilization and secretion
additional information
-
three-dimensional enzyme structure, overview
additional information
-
secondary structure of pure G6PI is estimated using circular dichroism to further predict the proper folding form of the protein
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purified recombinant enzyme with or without glucose 6-phosphate, sitting-drop vapor diffusion method, from 0.1 M Na-HEPES, pH 7.5, and 1.4 M tri-sodium citrate, 2 days, X-ray diffraction structure determination and analysis at 1.56-1.78 A resolution, molecular replacement using the structure of porcine PGI (PDB ID 1GZD) as a search model, modeling
enzyme structure analysis of unliganded and substrate-bound structures of Bdellovibrio bacteriovorus PGI solved to 1.74 A and 1.67 A resolution, respectively. Molecular replacement using PDB 1B0Z from Geobacillus stearothermophilus as a search model
-
hanging drop vapor diffusion method, crystal strcuture at 2.3 A resolution
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5 A and 2.3 A resolution, respectively. The inhibitors bind to a region within the domains interface and interact with His306 from the other subunit
molecular modeling and dynamics simulation of GTP binding
-
purified recombinant human PGI in complex with inhibitor N-(5-phospho-D-arabinoyl)-2-(amino)ethanamine, hanging drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein without or with 5 mM of inhibitor in 50 mM sodium chloride, and 20 mM Tris, pH 7.5 with 0.001 ml of crystallization solution containing 28-32% PEG 4000, 200 mM magnesium chloride, and 100 mM Tris, pH 8.5, in a 1:1 ratio, equilibration against a well of 0.5 ml crystallization solution at 18 C, X-ray diffraction structure determination and analysis at 1.95-2.38 A resolution, structure modeling, molecular replacement using the structure of hPGI at 1.6 A resolution (PDB ID 1IAT) as template
native enzyme and enzyme lacking N-terminal 47 amino acids. Comparison of data with mammalian enzymes
-
native enzyme and in complex with glucose 6-phosphate or erythrose 4-phosphate
hanging drop vapor diffusion method, using 1.2 M ammonium sulfate pH 8.5 (0.1 M HEPES) and 5% (v/v) glycerol at 10°C
resolution of 2.8 A, space group I212121
-
enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution
in complex with D-sorbitol 6-phosphate
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing 0.002 ml of both protein solution and reservoir solution, the latter containing 38% v/v PEG 400 and 0.2 M calcium acetate in 0.1 M sodium cacodylate-HCl, pH 6.5, equilibration over 0.5 ml of reservoir solution, 1 week, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
both native form and in complex with 5-phosphoarabinonate
1.9 A resolution, crystals belong to the space group P2(1)
hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Maximum resolution of 1.92 A on a single selenomethionine-incorporated crystal. Crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b = 42.4, c = 57.3 A, beta = 120.6° and a monomer in the asymmetric unit
-
in presence of bound zinc, substrate D-fructose 6-phosphate and several competitive inhibitors
native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+
structure is determined by X-ray diffraction to 2 A resolution
-
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate
enzyme complexed with glucose 6-phosphate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
purified enzyme with or without complexed glucose 6-phosphate, hanging drop vapour diffusion method, mixing of 0.0015 ml of 6 mg/ml protein solution with 0.0015 ml crystallization solution, and equilibration against 0.5 ml of reservoir solution, seeding, method screening and optimzation, 18°C, X-ray diffraction structure determination and analysis, comparison of crystal structures of isozymes TaPGIc and TaPGIp, overview
purified recombinant His-tagged enzyme complexed with glucose 6-phosphate, by hanging drop vapor diffusion method at room temperature, 0.004 ml of protein solution with 28.4 mg/ml protein and 5 mM fructose 6-phosphate is mixed with 0.002 ml of reservoir solution containing 10% PEG 3350, 50 mM sodium citrate, and 50 mM dithiothreitol, a few days, X-ray diffraction structure determination and analysis at 1.6 A resolution. Although fructose 6-phosphate is added to the crystallization mixture, the enzyme shows bound gluose 6-phosphate at its active site in the crystals
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E93A
Ni2+ content and apparent Ni2+ binding ability is reduced
E93D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
G79A
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
G79L
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
H136A
catalytic efficiency remains about the same compared to wild-type activity
H80A
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H80D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H82A
catalytic efficiency is reduced by more than 15fold, catalytic efficiency is reduced by more than 15fold. Ni2+ content and apparent Ni2+ binding ability is reduced
T63A
catalytic efficiency is reduced by more than 15fold
Y160F
catalytic efficiency is reduced by more than 15fold
Y95F
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
Y95K
catalytic efficiency is reduced by more than 15fold
G189E
-
GroD1 enzyme mutant cells show 87% reduced enzyme activity and defects in glycerolipid biosynthesis, overview. The phenotype comprises profound reduction in the synthesis of phosphatidylcholine, phosphatidylethanolamine, and triglycerides but high levels of phosphatidic acid and normal levels of phosphatidylinositol synthesis, accompanied by a reduction in phosphatidate phosphatase 1 activity. Expression of wild-type hamster GPI restores GPI activity, glycerolipid biosynthesis, and PAP1 activity in GroD1
A300P
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
A346H
-
mutation identified in a patient suffering from chronic nonspherocytic hemolytic anemia. Loss of 82% of enzyme activity, loss of enzyme capability to dimerize. Mutation results in significant changes in erythrocyte metabolism
D511N
the mutant shows 0.44% activity compared to the wild type enzyme
E495Q
the mutant shows 0.39% activity compared to the wild type enzyme
H100L
the mutant shows 0.16% activity compared to the wild type enzyme
H389R
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
H396L
the mutant shows 4.2% activity compared to the wild type enzyme
L487F
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
N154Q
the mutant shows 26% activity compared to the wild type enzyme
N386A
the mutant shows 36% activity compared to the wild type enzyme
Q343R
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
Q388A
the mutant shows 5.3% activity compared to the wild type enzyme
R273H
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
R472H
the mutation weakens network bonding of the enzyme
R539N
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
R75G
the mutation weakens network bonding of the enzyme
R83W
the mutation increases the water-accessible hydrophobic surface
S185A
the mutant shows 29% activity compared to the wild type enzyme
T224M
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
T375R
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T5I
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
V101M
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
Y274F
the mutant shows 46% activity compared to the wild type enzyme
Y341F
the mutant shows 65% activity compared to the wild type enzyme
Q111K
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
Q35H
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
Q35H/T49M
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
Q35H/T49M/V64I
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
S241A
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
T49M
-
site-directed mutagenesis, the mutant is more temperature-sensitive than the wild-type enzyme at 50°C
T49M/V64I
-
site-directed mutagenesis, the mutant is more temperature-sensitive than the wild-type enzyme at 50°C
V64I
-
site-directed mutagenesis, the mutant shows altered thermostability compared to wild-type enzyme
G157Y
the mutation results in a complete loss of activity
T211A
the mutant shows decreased activity with higher Km compared with that of the wild type protein
G157Y
-
the mutation results in a complete loss of activity
-
T211A
-
the mutant shows decreased activity with higher Km compared with that of the wild type protein
-
E98V
the ratio of turnover number and Km-value is 31373fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H137A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H89A
the ratio of turnover number and Km-value is 2712fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H91A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
E281A
site-directed mutagenesis, inactive mutant
E281A/H310A
site-directed mutagenesis, inactive mutant
E281A/Q415A
site-directed mutagenesis, inactive mutant
E281S
site-directed mutagenesis, inactive mutant
H310A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
H310A/K422A
site-directed mutagenesis, inactive mutant
K422A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
Q415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
E281A
-
site-directed mutagenesis, inactive mutant
-
E281A/H310A
-
site-directed mutagenesis, inactive mutant
-
E281A/Q415A
-
site-directed mutagenesis, inactive mutant
-
E281S
-
site-directed mutagenesis, inactive mutant
-
H310A/K422A
-
site-directed mutagenesis, inactive mutant
-
E281A
-
site-directed mutagenesis, inactive mutant
-
E281A/H310A
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site-directed mutagenesis, inactive mutant
-
E281A/Q415A
-
site-directed mutagenesis, inactive mutant
-
E281S
-
site-directed mutagenesis, inactive mutant
-
H310A/K422A
-
site-directed mutagenesis, inactive mutant
-
E281A
-
site-directed mutagenesis, inactive mutant
-
E281A/H310A
-
site-directed mutagenesis, inactive mutant
-
E281A/Q415A
-
site-directed mutagenesis, inactive mutant
-
E281S
-
site-directed mutagenesis, inactive mutant
-
H310A/K422A
-
site-directed mutagenesis, inactive mutant
-
E281A
-
site-directed mutagenesis, inactive mutant
-
E281A/H310A
-
site-directed mutagenesis, inactive mutant
-
E281A/Q415A
-
site-directed mutagenesis, inactive mutant
-
E281S
-
site-directed mutagenesis, inactive mutant
-
H310A/K422A
-
site-directed mutagenesis, inactive mutant
-
H391A
site-directed mutagenesis inactive mutant
H391K
site-directed mutagenesis inactive mutant
Q356A
site-directed mutagenesis inactive mutant
A221Q

site-directed mutagenesis
A221Q
-
site-directed mutagenesis
-
E495K

the mutation weakens network bonding of the enzyme
E495K
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
I525T

the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
I525T
the mutation destabilizes the ternary structure of the enzyme
L339P

the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
L339P
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
R347C

the mutation weakens network bonding of the enzyme
R347C
the mutation destabilizes the ternary structure of the enzyme
R347H

the mutation weakens network bonding of the enzyme
R347H
the mutation destabilizes the ternary structure of the enzyme
S278L

the mutation at or near the active site highly affects the catalytic efficiency of the enzyme
S278L
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T195I

the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T195I
the mutation destabilizes the ternary structure of the enzyme
additional information

loss of PGI1 impairs the conversion of F6P of the Calvin-Benson cycle to glucose 6-phosphate (G6P) for the synthesis of transitory starch in leaf chloroplasts. Since cpgi knockout mutants have not yet been obtained, they are thought to be lethal. The cpgi lethality can be rescued by expressing CaMV 35S promoter (p35S)-driven cPGI. But the complemented line is completely sterile due to pollen degeneration. A cpgi mutant expressing p35S::cPGI-YFP, in which YFP fluorescence in developing anthers, is undetectable specifically in the tapetum and in pollen, which can be associated with male sterility. RNAi-cPGI knockdown lines with strong cPGI repression in floral buds are generated that exhibit reduced male fertility due to the degeneration of most pollen. In wild-type background, six of the transformants produce mostly seedless siliques. The markedly reduced fertility is also associated with pollen degeneration, which is similar to the phenotypes of p35S::cPGI-YFP cpgi-3(-/-) plants. Histological analyses indicate that the synthesis of intersporal callose walls is impaired, causing microsporocytes to fail to separate haploid daughter nuclei to form tetrads, which might be responsible for subsequent pollen degeneration. cpgi knockout mutantsare isolated in the progeny of a heterozygous cpgi mutant floral-dipped with sugar solutions. The rescued cpgi mutants exhibit diminished young vegetative growth, reduced female fertility, and impaired intersporal callose wall formation in a meiocyte, and, thus, male sterility
additional information
the pgi deletion affects homeostasis of intracellular nucleotide sugars and phosphate sugars, cell wall contents are altered in the DELTApgi strain
additional information
-
the pgi deletion affects homeostasis of intracellular nucleotide sugars and phosphate sugars, cell wall contents are altered in the DELTApgi strain
-
additional information
-
mutant with point mutation in enzyme gene shows abnormal development after germination by extending a primary germ tube that quickly reverts to siotropic growth and results in an enlarged, swollen apex with pronounced wall thickenings. Mutant is unable to conidiate due to a block in conidiophore development at vesicle formation
additional information
-
independently isolated GPI-deficient mutants displayed similar phenotypes like G189E with respect to PAP1 activity and glycerolipid biosynthesis
additional information
identification of 33 single nucleotide polymorphisms and 14 insertion/deletion sites in the strain and EtG6-PI coding sequence
additional information
-
identification of 33 single nucleotide polymorphisms and 14 insertion/deletion sites in the strain and EtG6-PI coding sequence
additional information
-
construction of FgGPI deletion mutant, DELTAFgGPI phenotype, overview. The mutant shows reduced sensitivity to oxidative stress compared to wild-type, the intracellular H2O2 level is significantly reduced, while the sensitivity to Congo Red, fludioxonil, and carbendazim is unaltered. The expression of genes involved in glycolysis and pentose phosphate pathway is significantly reduced
additional information
-
construction of FgGPI deletion mutant, DELTAFgGPI phenotype, overview. The mutant shows reduced sensitivity to oxidative stress compared to wild-type, the intracellular H2O2 level is significantly reduced, while the sensitivity to Congo Red, fludioxonil, and carbendazim is unaltered. The expression of genes involved in glycolysis and pentose phosphate pathway is significantly reduced
-
additional information
-
downregulation of enzyme expression by siRNA results in increased sensitivity to oxidative stress and oxidative stress-induced cellular senescence. The senscence pathway involving p21 cyclin-dependent kinase inhibitor is up-regulated in enzyme knock-down cells
additional information
thermoinactivation of GPI genetic variants, phenotypes, overview
additional information
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thermoinactivation of GPI genetic variants, phenotypes, overview
additional information
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ectopic expression of PGI/AMF induces epithelial-to-mesenchymal transition in MCF10A epithelial breast cancer cells. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
additional information
construction of a lepgi-silenced strain using the lepgi-silencing vector and pAN7-ura3-dual vector without lepgi fragments (control) for transformation of Lentinula edodes strain LE69, phenotype, overview. The biomass of the mutant strains lepgii20 and lepgii27 is similar, and the biomass of both strains is much lower than that of the wild-type, which decreases by approximately 30%-70%. The content of extracellular polysacchrides (EPS) in lepgi strains is approximately 1.5 to 2fold higher than that in the wild-type and si-control. The intracellular polysacchrides (IPS) concentration of the lepgi strains increases by approximately 1.5fold compared with that of the wild-type and si-control. Moreover, lepgii20 and lepgii27 are very similar regarding their contents of both EPS and IPS. Altered cell wall composition. The expression levels of the genes that participate in the synthesis of beta-1,3-glucan drop by approximately 20%-70%, while the expression levels of genes responsible for chitin synthesis increase by 1.5 to 4fold in the mutant strains
additional information
-
construction of a lepgi-silenced strain using the lepgi-silencing vector and pAN7-ura3-dual vector without lepgi fragments (control) for transformation of Lentinula edodes strain LE69, phenotype, overview. The biomass of the mutant strains lepgii20 and lepgii27 is similar, and the biomass of both strains is much lower than that of the wild-type, which decreases by approximately 30%-70%. The content of extracellular polysacchrides (EPS) in lepgi strains is approximately 1.5 to 2fold higher than that in the wild-type and si-control. The intracellular polysacchrides (IPS) concentration of the lepgi strains increases by approximately 1.5fold compared with that of the wild-type and si-control. Moreover, lepgii20 and lepgii27 are very similar regarding their contents of both EPS and IPS. Altered cell wall composition. The expression levels of the genes that participate in the synthesis of beta-1,3-glucan drop by approximately 20%-70%, while the expression levels of genes responsible for chitin synthesis increase by 1.5 to 4fold in the mutant strains
-
additional information
-
identification of 3 amino acid substitutions in phosphoglucose isomerase (PGI) that are related to thermostability in the Glanville fritillary butterfly (Melitaea cinxia). After incubation at 50°C for 60 min, mutant G3-PGI-T49M exhibits a significantly higher activity loss rate than wild-type G3-PGI, whereas the other mutant PGIs show a similar activity loss rate to G3-PGI. The activity loss rates of all mutant PGIs are significantly lower than that of D1-PGI
additional information
-
recombinant enzyme carrying His-tag shows enzymatic acitivity equal to native enzyme
additional information
-
recombinant enzyme carrying His-tag shows enzymatic acitivity equal to native enzyme
-
additional information
because the C-terminus plays an essential role in stabilizing the dimer, a series of truncation mutants are constructed. Deletion of the last 13 amino acids in mutant PGIcD555-567, which are flexible in structure, do not affect its dimeric state and activity. Truncation before the last alpha-helix of PGIc in mutant PGIcD545-567 results in protein aggregation and abolished activity, whereas truncation before the last two alpha-helices (mutant PGIcD510-567) results in monomers with abolished activity. TaPGIc transgenic plants accumulate more starch, and increased biomass and seed yields concomitant with enhancement of photosynthesis
additional information
because the C-terminus plays an essential role in stabilizing the dimer, a series of truncation mutants are constructed. Deletion of the last 13 amino acids in mutant PGIcD555-567, which are flexible in structure, do not affect its dimeric state and activity. Truncation before the last alpha-helix of PGIc in mutant PGIcD545-567 results in protein aggregation and abolished activity, whereas truncation before the last two alpha-helices (mutant PGIcD510-567) results in monomers with abolished activity
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54.8
the melting temperature of the mutant is 54.8°C
75
purified native enzyme, half-life is 41 h
77
Tm-value of mutant enzyme G79L
85
purified native enzyme, half-life is 19 h
87
Tm-value of mutant enzyme G79A
98
Tm-value of wild-type enzyme and mutant enzymes T63A, H80A, H80D, H82A, E93A, E93D, Y95K and Y160F
100

melting temperature above 100°C
100
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3 min, complete loss of activity
100
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melting temperature for thermal unfolding, 60 min, 50% residual activity
100
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pH 7.0, 180 min, about 60% loss of activity
45

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soluble enzyme, t1/2: 42 min. Immobilized enzyme, t1/2: 82 min
45
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presence of Mn2+, 45 min, 55% loss of activity
45
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15 min, enzyme form PGI I, 50% loss of activity
50

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7 h, stable
50
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loss of about 25% activity for the Chinese allele g3 enzyme, G3-PGI, and of 50% for the Finnish allele D1 enzyme, D1-PGI, after 1 h
50
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30 min, no loss of activity
50
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soluble enzyme, t1/2: 12 min. Immobilized enzyme, t1/2: 10 min
55

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30 min, complete inactivation
55
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soluble enzyme, t1/2: 2 min. Immobilized enzyme, t1/2: 1 min
55
-
50% loss of activity, enzyme form PGI II
55
-
15 min, complete loss of activity
55
-
15 min, 50% loss of activity
60

-
free phosphoglucose isomerase is stable at a high protein concentration of 0.1 g/l (half-life of 180 h at 60°C) but deactivates rapidly at low concentrations (half-life at 60°C is 2.4 h at 0.001 g/l). Immobilized cellulose-binding module-phosphoglucose isomerase at a low concentration of 0.001 g/l has a half-life of 190 h, approximately 80fold of that of free phosphoglucose isomerase. Immobilized cellulose-binding module-phosphoglucose isomerase on regenerated amorphous cellulose is extremely stable at about 60°C, nearly independent of its mass concentration in bulk solution
60
-
15 min, 90% loss of activity
65

-
25% loss of activity after 1 h
65
purified native enzyme, half-life is 170 h
70

-
pH 7.0, 180 min, about 10% loss of activity
70
purified native enzyme, half-life is 68 h
80

-
120 min, stable
80
-
pH 7.0, 180 min, about 20% loss of activity
80
purified native enzyme, half-life is 25 h
90

-
120 min, about 40% loss of activity
90
-
pH 7.0, 180 min, about 50% loss of activity
90
purified native enzyme, half-life is 11 h
90
-
the enzyme exhibits a half-life of 40 min at 90°C
95

-
120 min, about 90% loss of activity
95
purified native enzyme, half-life is 7.9 h
97

-
melting temperature
97
Tm-value of mutant enzyme H136A
additional information

thermoinactivation of GPI genetic variants, overview
additional information
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thermoinactivation of GPI genetic variants, overview
additional information
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after incubation at 50°C for 60 min, mutant G3-PGI-T49M exhibits a significantly higher activity loss rate than wild-type G3-PGI, whereas the other mutant PGIs show a similar activity loss rate to G3-PGI. The activity loss rates of all mutant PGIs are significantly lower than that of D1-PGI
additional information
thermal inactivation follows first-order kinetics
additional information
-
thermal inactivation follows first-order kinetics
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DNA and amino acid sequence determination and analysis, GPI expression analysis, recombinant expression of the enzyme in Escherichia coli strain BL21
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogeneitic analysis, and genotyping for polymorphisms
DNA and amino acid sequence determination, PGI genotyping for polymorphisms, influence of environmental conditions and geographic genetic structuring, modeling, overview
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expressed in Escherichia coli BL21 Star (DE3) cells
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expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
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expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli BL21
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant enzymes in Escherichia coli strain DF2145
functionally expressed in Escherichia coli BL21(DE3)
gene lepgi, sequence comparisons, quantitative real-time PCR enzyme expression analysis
gene pgi or AFUB_025630, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli
gene pgi, DNA and amino acid sequence determination and analysis, 5 alleles are found in the Finnish population, with pgi-d1 being the most common allele, while 2 alleles are found in the Chinese population, with the newly discovered pgig3 allele as the most common, sequence comparisons, recombinant expression of His-tagged enzyme from alleles pgi-d1 and pgig3 in Escherichia coli strain BL21(DE3)
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gene pgi, DNA and amino acid sequence determination and analysis, six PGI gene loci are found in the wheat genome and they are named as TaPGIc1AS, TaPGIc1BS, TaPGIc1DS, TaPGIp5AL, TaPGIp5BL and TaPGIp5DL according to their protein subcellular locations as indicated with a lowercase letter (c for cytosol and p for plastid) and gene locations on chromosome. Three PGI genes located on chromosome 5 encode proteins predicted to localize to plastids, while the remaining three genes located on the chromosome 1 encode proteins predicted to localize to the cytosol. Wheat plastidic and cytosolic PGIs share about 24% identity, but the identity jumps to 98% within each of those groups. Recombinant expression of isozyme TaPGIc under control of the constitutively active S35 promoter in an T-DNA insertion mutant of Arabidopsis thaliana. T-DNA fragment is inserted into the 11th exon of AtPGIp gene, resulting in the deletion of the last 118 amino acids and enzymatic inactivity. T-DNA fragment is inserted into the 11th exon of AtPGIp gene, resulting in the deletion of the last 118 amino acids and enzymatic inactivity. Arabidopsis pgip mutant plant exhibit macroscopic growth retardation compared with wild-type, while the transformed gene TaPGIc can rescue the phenotype at seeding stage, and the transgenic plant shows noticeably more biomass prior to harvest. Quantitative RT-PCR enzyme expression analysis
gene pgi, DNA and amino acid sequence determination and analysis, six PGI gene loci are found in the wheat genome and they are named as TaPGIc1AS, TaPGIc1BS, TaPGIc1DS, TaPGIp5AL, TaPGIp5BL and TaPGIp5DL according to their protein subcellular locations as indicated with a lowercase letter (c for cytosol and p for plastid) and gene locations on chromosome. Three PGI genes located on chromosome 5 encode proteins predicted to localize to plastids, while the remaining three genes located on the chromosome 1 encode proteins predicted to localize to the cytosol. Wheat plastidic and cytosolic PGIs share about 24% identity, but the identity jumps to 98% within each of those groups. Recombinant expression of isozyme TaPGIp under control of the constitutively active S35 promoter in an T-DNA insertion mutant of Arabidopsis thaliana. T-DNA fragment is inserted into the 11th exon of AtPGIp gene, resulting in the deletion of the last 118 amino acids and enzymatic inactivity. Arabidopsis pgip mutant plant exhibit macroscopic growth retardation compared with wild-type, while the transformed gene TaPGIp can rescue the phenotype at seeding stage, and the transgenic plant shows noticeably more biomass prior to harvest. Quantitative RT-PCR enzyme expression analysis
gene pgi, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain HK100, subcloning in Escherichia coli TOP 10 cells
gene pgi, recombinant expression of the cPGI-YFP fusion protein in the PGI deletion mutant, generation of cPGI overexpressing lines (p35S::cPGI-YFP transgenic plants in either wild-type or cpgi-3 +/- background, cPGI-ox). YFP signals are undetectable restrictedly in the tapetum and pollen in developing anthers of p35S::cPGI-YFP cpgi-3(-/-) plants
genotyping and polymorphisms, overview
GPI gene, DNA and amino acid sequence determination and analysis, phylogenetic tree and expression analysis by real time quantitative RT-PCR, recombinant expression of His-tagged enzyme in Escherichia coli
isozyme A and B overexpressed in Escherichia coli
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native enzyme and mutant enzymes T5I, T224M, Q343R, D539N
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overexpressed in Escherichia coli
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overexpression in Escherichia coli
overexpression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
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PGI, expression analysis in cells from healthy and colon cancer individuals
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quantitative RT-PCR enzyme expression analysis, recombinant expression of GFP-tagged wild-type enzyme in Fusarium graminearum strain 2021
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recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), enzyme G6PI production in a self-inducible construct in the bacterial expression system
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-

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expression in Escherichia coli

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expression in Escherichia coli
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genotyping and polymorphisms, overview

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genotyping and polymorphisms, overview
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genotyping and polymorphisms, overview
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overexpression in Escherichia coli

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overexpression in Escherichia coli
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