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1,5-Anhydroglucitol 6-phosphate
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2-amino-2-deoxy-D-glucitol 6-phosphate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-glucitol 6-phosphate dimethyl ester
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-mannitol 6-phosphate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-Deoxy-D-glucitol 6-phosphate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-deoxyglucose 6-phosphate
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5-deoxy-5-malonate-D-arabinonohydroxamic acid
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5-phospho-D-arabinoamide
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinoate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinohydroxamate
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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
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5-phosphoarabinonhydroxamic acid
6-phospho-2-deoxygluconate
Cassia coluteoides
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glucose 6-phosphate as substrate
6-phospho-D-gluconate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phospho-D-gluconoamide
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-Phosphomannonate
Cassia coluteoides
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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
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
dihydroxyacetone phosphate
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Erythritol 4-phosphate
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erythrose-4-phosphate
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gluconate 6-phosphate
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glyceraldehyde 3-phosphate
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GTP
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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
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both glycosylated and unglycosylated, binding and inhibition of enzyme
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K+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
L-Sorbose 6-phosphate
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L-xylulose 5-phosphate
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Maleate
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10 mM, 50% inhibition
malonate
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10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
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glucose 6-phosphate as substrate
N,2,3,4,5-pentahydroxypentanamide
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N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
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comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
N-bromoacetylethanolamine phosphate
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oxaloacetate
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10 mM, 25% inhibition
oxoglutarate
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10 mM, 20% inhibition
sedoheptulose 7-phosphate
5-phospho-D-arabinonate
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5-phospho-D-arabinonate
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5-phospho-D-arabinonate
competitive
5-phosphoarabinonhydroxamic acid
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5-phosphoarabinonhydroxamic acid
competitive inhibition
6-phosphogluconate
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6-phosphogluconate
Cassia coluteoides
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glucose 6-phosphate as substrate
6-phosphogluconate
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0.2 mM, 52% inhibition
6-phosphogluconate
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competitive
6-phosphogluconate
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pH 7.6, 25°C
6-phosphogluconate
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competitive
Agaricic acid
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Agaricic acid
irreversible inhibition
Cd2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
Cu2+
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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
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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
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D-gluconate 6-phosphate
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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
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EDTA
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
EDTA
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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
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erythrose 4-phosphate
Cassia coluteoides
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glucose 6-phosphate as substrate
erythrose 4-phosphate
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0.02 mM, 58% inhibition
erythrose 4-phosphate
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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
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competitive
erythrose 4-phosphate
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erythrose 4-phosphate
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erythrose 4-phosphate
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erythrose 4-phosphate
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competitive
fructose 1,6-diphosphate
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1 mM, 4% inhibition
fructose 1,6-diphosphate
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fructose 1-phosphate
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1 mM, 10% inhibition
Hg2+
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1 mM, about 50% inhibition
Mn2+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
Ni2+
10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
phosphate
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ribose 5-phosphate
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1 mM, 12% inhibition
ribulose 5-phosphate
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0.5 mM, 48% inhibition
sedoheptulose 7-phosphate
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1 mM, 10% inhibition
sedoheptulose 7-phosphate
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sorbitol-6-phosphate
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suramin
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no inhibition
suramin
an anti-trypanosomal drug
Zn2+
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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
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no inhibition by PCMB and iodoacetate
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additional information
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screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
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additional information
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not inhibitory: EDTA
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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
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additional information
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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
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additional information
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no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
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