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(1R,2R)-1-O-(2-acetylamino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate) + H2O
?
-
-
-
-
?
1-D-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-myo-inositol 1-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate) + H2O
?
-
-
-
-
?
2-acetamido-2-deoxy-alpha-D-glucopyranosyl-(1->6)-phosphatidylinositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
6-(N-butanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + butanoate
6-(N-hexanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + hexanoate
6-(N-isobutanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + isobutanoate
6-(N-pentanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + pentanoate
6-(N-propionyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + propionate
D-GlcNAc-alpha(1->6)-D-myo-inositol-1-octadecyl phosphate + H2O
D-GlcN-alpha(1->6)-D-myo-inositol-1-octadecyl phosphate + acetate
-
-
-
-
?
D-GlcNAc-alpha1-6-D-myo-inositol-1-HPO4-3-sn-1,2-diacylglycerol + H2O
?
-
-
-
-
?
N,N-diethylethanaminium 1-D-2-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-myo-inosityl octadecyl phosphate + H2O
?
-
-
-
-
?
N-acetyl-D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + H2O
D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + acetate
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
?
-
involved in the formation of the glycosylphosphatidylinositol membrane anchor of the trypanosome variant-surface glycoprotein
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
N-acetyl-D-glucosaminylphosphatidylinositol + H2O + H2O
D-glucosaminylphosphatidylinositol + acetate
-
-
-
-
?
additional information
?
-
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
the substrate is prepared from Saccharomyces cerevisiae microsomes. [6-3H]GlcN-PI is converted to [6-3H]GlcNAc-PI using anhydride
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
the substrate is prepared from Saccharomyces cerevisiae microsomes. [6-3H]GlcN-PI is converted to [6-3H]GlcNAc-PI using anhydride
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
the phosphate, 2'-NHAc and 3'-OH groups of the natural substrate alpha-D-GlcpNAc-PI are critical for recognition by the Trypanosoma brucei GlcNAc-PI de-N-acetylase
-
-
?
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
substrate binding analysis by docking with Zn2+ to the enzyme's active site
-
-
?
6-(N-butanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + butanoate
-
very poor substrate
-
?
6-(N-butanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + butanoate
-
-
-
?
6-(N-hexanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + hexanoate
-
-
-
?
6-(N-hexanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + hexanoate
-
-
-
?
6-(N-isobutanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + isobutanoate
-
poor substrate
-
?
6-(N-isobutanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + isobutanoate
-
-
-
?
6-(N-pentanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + pentanoate
-
-
-
?
6-(N-pentanoyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + pentanoate
-
-
-
?
6-(N-propionyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + propionate
-
-
-
?
6-(N-propionyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + propionate
-
-
-
?
N-acetyl-D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + H2O
D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + acetate
-
synthetic substrate
-
-
?
N-acetyl-D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + H2O
D-glucosamine-alpha-(1-6)-D-myo-inositol-1-octadecyl phosphate + acetate
-
synthetic substrate
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
-
-
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
-
-
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
37°C, pH 7.4, 25 mM KCl, 5 mM MgCl2, 5 mM MnCl2, 0.5 mM dithiothreitol, 0.1 mM 1-chloro-3-tosylamido-7-amino-2-heptanone, 1 microg/ml leupeptin
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
37°C
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
30°C, pH 7.4, 50 mM KCl, 10 mM dithiothreitol, 0.1 mM 1-chloro-3-tosylamido-7-amino-2-heptanone, 1 microg/ml leupeptin
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
-
-
-
?
N-Acetyl-D-glucosaminylphosphatidylinositol + H2O
D-Glucosaminylphosphatidylinositol + acetate
-
analogues lacking the glycerophosphate component are not recognized
-
?
additional information
?
-
the enzyme shows an overall low activity
-
-
-
additional information
?
-
-
the enzyme shows an overall low activity
-
-
-
additional information
?
-
the enzyme shows an overall low activity
-
-
-
additional information
?
-
-
no substrate: mannosylated N-acetyl-D-glucosylphosphatidylinositol-derivatives
-
?
additional information
?
-
-
structural requirements of substrate, enzyme cannot act on analogues containing N-benzoyl-, N-acetyl-D-galactosyl- or N-acetyl-beta-D-glucosyl-groups
-
?
additional information
?
-
-
structural requirements of substrate, enzyme cannot act on substrate analogues containing N-acetyl-beta-glucosyl-groups or aromatic N-acyl groups
-
?
additional information
?
-
-
structural requirements of substrate, enzyme can act on analogues containing N-benzoyl-, N-acetyl-D-galactosyl- or N-acetyl-beta-D-glucosyl-groups
-
?
additional information
?
-
-
structural requirements of substrate, enzyme can act on substrate analogues containing N-acetyl-beta-glucosyl-groups or aromatic N-acyl groups
-
?
additional information
?
-
-
substrate specificity in decreasing order: N-acetyl-D-glucosylphosphatidylinositol, N-propionylglucosylphosphatidylinositol, N-butyrylglucosylphosphatidylinositol, N-isobutyrylglucosylphosphatidylinositol, N-pentanoylglucosylphosphatidylinositol, N-hexanoylglucosylphosphatidylinositol, no substrate: mannosylated N-acetyl-D-glucosylphosphatidylinositol-derivatives
-
?
additional information
?
-
-
synthesis of substrate analogues and substrate structure-activity analysis, molecular dynamics simulations, overview. (1R,2R)-1-O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate) is neither a substrate nor an inhibitor. No recognition and activity with substrate analogues (1R,2R)-2-[(2-amino-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate, (1R,2R)-2-[(2-amino-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate, (1R,2R)-1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate), (1R,2R)-1-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate), N-(1R,2R)-2-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-cyclohexyloctadecane-1-sulphonamide, N-(1R,2R)-2-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexyloctadecane-1-sulphonamide, and triethylammonium trans-2-(2-amino-3-hydroxypropoxy)-cyclohexyl n-octadecyl phosphate, as well as with (1R,2R)-2-[(2-acetylamino-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate, (1R,2R)-2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate, (1R,2R)-1-O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate), N-((1R,2R)-2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl)octadecane-1-sulfonamide, N-((1R,2R)-2-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl)octadecane-1-sulfonamide, and N,N-diethylethanaminium (1R,2R)-2-(2-acetamido-3-hydroxypropoxy)cyclohexyl octadecyl phosphate. The requirement for the presence of inositol 2-, 3-, 4-, and 5-OH groups for recognition by the enzyme is nuanced and may depend on the conformational flexibility of the substrate analogue. The glucosamine and the phospholipid moieties are essential for binding and, while the D-myo-inositol residue is the preferred aglycone for recognition by the enzyme, the dispensing of it entirely with a cyclohexanediol group is tolerated by the enzyme
-
-
?
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(1R,2R)-1-O-(2-acetylamino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate)
-
competitive
(1R,2R)-1-O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate)
-
-
(1R,2R)-1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate)
-
-
(1R,2R)-1-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate)
-
-
(1R,2R)-2-((2-deoxy-2-[(hydroxycarbamoyl)amino]-beta-D-glucopyranosyl)oxy)cyclohexyl octadecyl phosphate
-
-
(1R,2R)-2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate
-
-
(1R,2R)-2-[(2-acetylamino-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate
-
-
(1R,2R)-2-[(2-amino-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate
-
-
(1R,2R)-2-[(2-amino-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl octadecyl phosphate
-
-
(1R,2R,3S,4R,5R,6R)-2-([2-deoxy-2-[(hydroxycarbamoyl)amino]-alpha-D-glucopyranosyl]oxy)-3,4,5,6-tetrahydroxycyclohexyl octadecyl hydrogen phosphate
-
-
(1R,2S,3R,4R,5R)-4-(prop-2-en-1-yl)-6,8-dioxabicyclo[3.2.1]octane-2,3-diyl diacetate
-
-
(2R)-3-{[{[(1R,2R,3S,4R,5R,6R)-2-{[2-(carbamoylamino)-2-deoxy-alpha-D-glucopyranosyl]oxy}-3,4,5,6-tetrahydroxycyclohexyl]oxy}(hydroxy)phosphoryl]oxy}propane-1,2-diyl dihexadecanoate
-
-
1,3,4,6-tetra-O-acetyl-2-C-allyl-2-deoxy-alpha-D-glucopyranose
-
-
1,3,4,6-tetra-O-acetyl-2-C-carboxymethyl-2-deoxy-alpha-D-glucopyranose
-
-
1,3,4,6-tetra-O-acetyl-2-deoxy-2-C-formylmethyl-alpha-Dglucopyranose
-
-
1,5-anhydro-2-(carboxymethyl)-2-deoxy-D-glucitol
-
-
1,5-anhydro-2-C-(carboxymethyl N-hydroxyamide)-2-deoxy-D-glucitol
-
-
1,5-anhydro-2-C-carboxymethyl-2-deoxy-D-glucitol
-
-
1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-3-O-phenyl-D-glucitol
-
-
1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-D-glucitol
-
-
1,5-anhydro-3-O-benzoyl-2-C-carboxymethyl-2-deoxy-D-glucitol
-
-
1,5-anhydro-3-O-benzyl-2-(carboxymethyl)-2-deoxy-D-glucitol
-
-
1,5-anhydro-3-O-benzyl-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-D-glucitol
-
-
1,5-anhydro-3-O-benzyl-4,6-O-benzylidene-2-(carboxymethyl)-2-deoxy-D-glucitol
-
-
1,5-anhydro-3-O-benzyl-4,6-O-benzylidene-2-[2-[(benzyloxy)amino]-2-oxoethyl]-2-deoxy-D-glucitol
-
-
1,5-anhydro-4,6-O-benzylidene-2-(carboxymethyl)-2-deoxy-D-glucitol
-
-
1,5-anhydro-4,6-O-benzylidene-2-deoxy-2-prop-2-en-1-yl-D-glucitol
-
-
1,5-anhydro-4,6-O-benzylidene-2-[2-[(benzyloxy)amino]-2-oxoethyl]-2-deoxy-D-glucitol
-
-
1-acetyl-N-[4-hydroxy-3-(hydroxycarbamoyl)phenyl]piperidine-4-carboxamide
-
40% inhibition at 1 mM
1-{1-[3-chloro-5-(trifluoromethyl)pyridin-2-yl]piperidin-4-yl}-2-hydroxyethan-1-one
-
-
2-(2,4-dichlorophenoxy)-N-hydroxyacetamide
-
-
2-(carboxymethyl)-2-deoxy-D-glucopyranose
-
-
2-C-carboxymethyl-2-deoxy-D-glucopyranose
-
-
2-deoxy-2-ureido-D-galactosylalpha1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
suicide inhibitor, 50% inihibition at 0.0002 mM
2-deoxy-2-ureido-D-glucosyl-alpha1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
2-deoxy-2-ureido-D-glucosyl-beta1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
50% inhibition at about 8 nM
2-deoxy-2-ureido-D-glucosylalpha1-6-D-(2-O-octyl)myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
50% inhibition at about 8 nM
2-deoxy-2-ureido-D-glucosylbeta1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
suicide inhibitor, 50% inihibition at 0.0002 mM
2-hydroxybenzoic acid
-
97% inhibition at 1 mM
3-[3-(4-chlorophenyl)-1,2,4-oxadiazol-5-yl]-N-hydroxypropanamide
-
-
4-(2,4-dichlorophenoxy)-N-hydroxybutanamide
-
-
4-bromo-N,2-dihydroxybenzamide
-
86% inhibition at 1 mM
4-bromo-N-hydroxybenzamide
-
9.6% inhibition at 1 mM
5-((tert-butoxycarbonyl)amino)-2-hydroxybenzoic acid
-
-
5-amino-N-(benzyloxy)-2-hydroxybenzamide
-
-
5-benzamido-N,2-dihydroxybenzamide
-
96% inhibition at 1 mM
5-[(cyclohexanecarbonyl)amino]-N,2-dihydroxybenzamide
-
99% inhibition at 1 mM
EDTA
complete inhibition at 10 mM, the enzyme irreversibly loses activity upon incubation with a metal chelator
ethambutol
docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness
metaraminol
docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness
N,2-dihydroxy-5-(4-methylbenzamido)benzamide
-
62% inhibition at 1 mM
N,2-dihydroxy-5-(octadecanoylamino)benzamide
-
25% inhibition at 1 mM
N,N-diethylethanaminium (1R,2R)-2-(2-acetamido-3-hydroxypropoxy)cyclohexyl octadecyl phosphate
-
-
N,N-diethylethanaminium 1-D-2-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-myo-inosityl octadecyl phosphate
-
-
N-((1R,2R)-2-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]cyclohexyl)octadecane-1-sulfonamide
-
-
N-((1R,2R)-2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)oxy]cyclohexyl)octadecane-1-sulfonamide
-
-
N-(1R,2R)-2-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-cyclohexyloctadecane-1-sulphonamide
-
-
N-(1R,2R)-2-O-(2-amino-2-deoxy-beta-D-glucopyranosyl)-cyclohexyloctadecane-1-sulphonamide
-
-
N-dimethyl-D-glucosyl-phosphatidylinositol
-
0.001 mM, complete inhibition
N-hydroxy-N'-(4-methoxyphenyl)urea
-
-
N-hydroxybenzamide
-
25% inhibition at 1 mM
N-[4-hydroxy-3-(hydroxycarbamoyl)phenyl]-2H-1,3-benzodioxole-5-carboxamide
-
86% inhibition at 1 mM
N-[4-hydroxy-3-(hydroxycarbamoyl)phenyl]oxane-4-carboxamide
-
56% inhibition at 1 mM
N-[4-hydroxy-3-(hydroxycarbamoyl)phenyl][1,1'-biphenyl]-4-carboxamide
-
75% inhibition at 1 mM
phenyl 2-(carbamoylamino)-2-deoxy-1-thio-beta-D-glucopyranoside
-
-
phenyl 2-(carboxymethyl)-2-deoxy-1-thio-alpha-D-glucopyranoside
-
-
phenyl 2-(N-aminocarbonyl)amino-2-deoxy-1-thio-beta-Dglucopyranoside
-
-
phenyl 2-amino-2-deoxy-1-thio-beta-D-glucopyranoside
-
-
phenyl 2-C-carboxymethyl-2-deoxy-1-thio-alpha-Dglucopyranoside
-
-
phenyl 2-C-carboxymethyl-2-deoxy-1-thio-beta-Dglucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-C-allyl-2-deoxy-1-thio-alpha-D-glucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-C-allyl-2-deoxy-1-thio-beta-D-glucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-C-carboxymethyl-2-deoxy-1-thio-alpha-D-glucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-C-carboxymethyl-2-deoxy-1-thio-beta-D-glucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-deoxy-2-C-formylmethyl-1-thio-alpha-D-glucopyranoside
-
-
phenyl 3,4,6-tri-O-acetyl-2-deoxy-2-C-formylmethyl-1-thio-beta-D-glucopyranoside
-
-
salicylic hydroxamic acid
-
enzyme inhibitor with high ligand efficiency, proposed mode of action, overview
tert-butyl (3-((benzyloxy)carbamoyl)-4-hydroxyphenyl)carbamate
-
-
triethylammonium 1R,2R-1-O-[2-C-(carboxymethyl N-hydroxyamide)-2-deoxy-beta-D-glucopyranosyl]-cyclohexanediol 2-(n-octadecylphosphate)
-
-
triethylammonium trans-2-(2-amino-3-hydroxypropoxy)-cyclohexyl n-octadecyl phosphate
-
-
2-deoxy-2-ureido-D-glucosyl-alpha1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
50% inhibition between 0.0001 and 0.001 mM
2-deoxy-2-ureido-D-glucosyl-alpha1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
50% inhibition at 8 nM
additional information
-
treatment with EDTA consistently causes up to 2% reduction in activity, the activity is not significantly affected by treatment with 1,10-phenanthroline
-
additional information
-
not inhibitory up to 0.1 mM: 2-deoxy-2-ureido-D-glucosyl-beta1-6-D-myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol, 2-deoxy-2-ureido-D-glucosylalpha1-6-D-(2-O-octyl)myo-inositol-1-phosphoryl-sn-1,2-dipalmitoylglycerol
-
additional information
-
inhibitor identification via zinc binding fragment screening, structure activity relationship, hydroxamic acid and 2-OH are essential for potency, substitution is tolerated at the 4- and 5-positions. No inhibition by 2-bromo-N-hydroxybenzamide and 2-amino-N-hydroxybenzamide
-
additional information
-
(1R,2R)-1-O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-cyclohexanediol 2-(1,2-di-O-hexadecanoyl-sn-glycerol 3-phosphate) is neither a substrate nor an inhibitor
-
additional information
inhibitor search by structural based virtual screening (SBVS), molecular modeling, and docking study, overview
-
additional information
-
inhibitor search by structural based virtual screening (SBVS), molecular modeling, and docking study, overview
-
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0.00137 - 0.00263
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
0.00015 - 0.00205
N-acetyl-D-glucosaminylphosphatidylinositol
0.00137
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant H140A cytoplasmic catalytic domain, metal added
0.0016
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant H140A cytoplasmic catalytic domain, no metal added
0.00182
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant D46A cytoplasmic catalytic domain, no metal added
0.00195
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant D46A cytoplasmic catalytic domain, metal added
0.00195
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant wild-type cytoplasmic catalytic domain, no metal added
0.00199
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant H43A cytoplasmic catalytic domain, no metal added
0.00209
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant wild-type cytoplasmic catalytic domain, metal added
0.00263
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
pH 5.5, 37°C, recombinant mutant H43A cytoplasmic catalytic domain, metal added
0.00015
N-acetyl-D-glucosaminylphosphatidylinositol
-
-
0.00195
N-acetyl-D-glucosaminylphosphatidylinositol
-
in the absence of metal ions, in 50 mM acetate buffer at pH 5.5 and 37°C
0.00205
N-acetyl-D-glucosaminylphosphatidylinositol
-
in the presence of 5 mM Mn2+, in 50 mM acetate buffer at pH 5.5 and 37°C
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10
1,5-anhydro-2-(carboxymethyl)-2-deoxy-D-glucitol
Trypanosoma brucei
-
IC50 above 10 mM, in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
10
1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-D-glucitol
Trypanosoma brucei
-
IC50 above 10 mM, in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
0.29
1,5-anhydro-3-O-benzyl-2-(carboxymethyl)-2-deoxy-D-glucitol
Trypanosoma brucei
-
in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
1.5
1,5-anhydro-3-O-benzyl-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-D-glucitol
Trypanosoma brucei
-
in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
0.3
2-(carboxymethyl)-2-deoxy-D-glucopyranose
Trypanosoma brucei
-
in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
10
phenyl 2-(carbamoylamino)-2-deoxy-1-thio-beta-D-glucopyranoside
Trypanosoma brucei
-
IC50 above 10 mM, in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
0.1 - 10
phenyl 2-(carboxymethyl)-2-deoxy-1-thio-alpha-D-glucopyranoside
0.063
salicylic hydroxamic acid
Trypanosoma brucei
-
pH 8.0, 37°C
0.019
triethylammonium 1R,2R-1-O-[2-C-(carboxymethyl N-hydroxyamide)-2-deoxy-beta-D-glucopyranosyl]-cyclohexanediol 2-(n-octadecylphosphate)
Trypanosoma brucei
-
in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
0.1
phenyl 2-(carboxymethyl)-2-deoxy-1-thio-alpha-D-glucopyranoside
Trypanosoma brucei
-
in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
10
phenyl 2-(carboxymethyl)-2-deoxy-1-thio-alpha-D-glucopyranoside
Trypanosoma brucei
-
IC50 above 10 mM, in 50 mM Na-HEPES pH 7.4, 25 mM KCl, 0.1 mM Tos-LysCH2Cl and 0.001 mg/ml leupeptin, at 30°C
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evolution
the predicted active site residues of the GPI domain are ultra-conserved for the Trypanosomatidae family. Structure comparions at the primary, secondary and tertiary level by alignment
malfunction
an in vitro study using murine MQ cell line J774 shows that by the use of recombinant parasites the entry rate and infecting ability is decreased. The mutant parasites are unable to produce skin lesions even six months post-infection in the BALB/c mice
malfunction
loss of the enzyme causes reduction of GlcNAc-PI de-N-acetylase activity, cell wall defects, and filamentation defects. The filamentation defects can be specifically correlated to an upregulation of the HOG1 pathway. In the CaGPI12 conditional null strain grown under repressive conditions, no pseudohyphae or hyphae formation is observed and all cells are in the yeast form in contrast to wild-type. The CaGPI12 conditional null mutant is resistant to azoles. Reintroduction of CaGPI12 in the CaGPI12 conditional null can reverse its growth defect and restore de-N-acetylase activity
malfunction
-
loss of the enzyme causes reduction of GlcNAc-PI de-N-acetylase activity, cell wall defects, and filamentation defects. The filamentation defects can be specifically correlated to an upregulation of the HOG1 pathway. In the CaGPI12 conditional null strain grown under repressive conditions, no pseudohyphae or hyphae formation is observed and all cells are in the yeast form in contrast to wild-type. The CaGPI12 conditional null mutant is resistant to azoles. Reintroduction of CaGPI12 in the CaGPI12 conditional null can reverse its growth defect and restore de-N-acetylase activity
-
malfunction
-
an in vitro study using murine MQ cell line J774 shows that by the use of recombinant parasites the entry rate and infecting ability is decreased. The mutant parasites are unable to produce skin lesions even six months post-infection in the BALB/c mice
-
malfunction
-
an in vitro study using murine MQ cell line J774 shows that by the use of recombinant parasites the entry rate and infecting ability is decreased. The mutant parasites are unable to produce skin lesions even six months post-infection in the BALB/c mice
-
malfunction
-
an in vitro study using murine MQ cell line J774 shows that by the use of recombinant parasites the entry rate and infecting ability is decreased. The mutant parasites are unable to produce skin lesions even six months post-infection in the BALB/c mice
-
malfunction
-
an in vitro study using murine MQ cell line J774 shows that by the use of recombinant parasites the entry rate and infecting ability is decreased. The mutant parasites are unable to produce skin lesions even six months post-infection in the BALB/c mice
-
metabolism
the enzyme functions at the second step of GPI anchor biosynthesis, converting N-acetylglucosaminylphosphatidylinositol to glucosaminylphosphatidylinositol. This step is conserved in the GPI biosynthesis pathway
metabolism
-
the enzyme is responsible for the second step in the glycosylphosphatidylinositol biosynthetic pathway of Trypanosoma brucei, which is a prerequisite for all subsequent steps in the pathway
metabolism
the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Candida albicans
metabolism
the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Trypanosoma brucei
metabolism
-
the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Candida albicans
-
physiological function
Candida albicans N-acetylglucosaminylphosphatidylinositol de-N-acetylase (CaGpi12) recognises N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) from Saccharomyces cerevisiae and is able to complement the Saccharomyces cerevisiae ScGPI12 function. CaGPI12 is able to rescue the growth defect of the ScGPI12 conditional null strain as compared to the control strain carrying the YepHIS vector alone, suggesting that CaGPI12 functionally complements ScGPI12. CaGPI12 is essential for growth and viability of Candida albicans. CaGPI12 is required for yeast to hyphal transition in Candida albicans
physiological function
GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Stationary phase promastigotes are used for in vitro cell line J774 macrophage infectivity test also for in vivo infection
physiological function
Trypanosoma brucei is a protozoan that causes African sleeping sickness in humans. Many glycoconjugate compounds are present on the entire cell surface of Trypanosoma brucei to control the infectivity and survival of this pathogen. These glycoconjugates are anchored to the plasma membrane with the help of glycosyl phosphatidyl inositol (GPI) anchors. This type of anchor is much more common in protozoans than in other eukaryotes. The second step of glycosyl phosphatidyl inositol (GPI) anchor biosynthesis is catalyzed by an enzyme, which is GlcNAc-PI de-N-acetylase. GlcNAc-PI de-N-acetylase has a conserved GPI domain, which is responsible for the functionality of this enzyme
physiological function
-
Candida albicans N-acetylglucosaminylphosphatidylinositol de-N-acetylase (CaGpi12) recognises N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) from Saccharomyces cerevisiae and is able to complement the Saccharomyces cerevisiae ScGPI12 function. CaGPI12 is able to rescue the growth defect of the ScGPI12 conditional null strain as compared to the control strain carrying the YepHIS vector alone, suggesting that CaGPI12 functionally complements ScGPI12. CaGPI12 is essential for growth and viability of Candida albicans. CaGPI12 is required for yeast to hyphal transition in Candida albicans
-
physiological function
-
GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Stationary phase promastigotes are used for in vitro cell line J774 macrophage infectivity test also for in vivo infection
-
physiological function
-
GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Stationary phase promastigotes are used for in vitro cell line J774 macrophage infectivity test also for in vivo infection
-
physiological function
-
GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Stationary phase promastigotes are used for in vitro cell line J774 macrophage infectivity test also for in vivo infection
-
physiological function
-
GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Stationary phase promastigotes are used for in vitro cell line J774 macrophage infectivity test also for in vivo infection
-
additional information
residues Asp46 and His140 of the enzyme are important for catalysis
additional information
-
residues Asp46 and His140 of the enzyme are important for catalysis
additional information
GlcNAc-PI de-N-acetylase has a conserved GPI domain, which is responsible for the functionality of this enzyme, three-dimensional enzyme structure modeling and ligand modelling, overview. The predicted active site residues are His41, Pro42, Asp43, Asp44, Met47, Phe48, Ser74, Arg80, His103, Val144, Ser145, His147 and His150. Two hydrogen bond acceptors and four hydrogen bond donors are found in the modelled pharmacophore
additional information
-
GlcNAc-PI de-N-acetylase has a conserved GPI domain, which is responsible for the functionality of this enzyme, three-dimensional enzyme structure modeling and ligand modelling, overview. The predicted active site residues are His41, Pro42, Asp43, Asp44, Met47, Phe48, Ser74, Arg80, His103, Val144, Ser145, His147 and His150. Two hydrogen bond acceptors and four hydrogen bond donors are found in the modelled pharmacophore
additional information
two conserved motifs, HPDDE and HXXH, are both important for the enzyme function in the cell. Enzyme structure comparison of CaGPI12 with Saccharomyces cerevisiae GPI12
additional information
-
two conserved motifs, HPDDE and HXXH, are both important for the enzyme function in the cell. Enzyme structure comparison of CaGPI12 with Saccharomyces cerevisiae GPI12
additional information
-
two conserved motifs, HPDDE and HXXH, are both important for the enzyme function in the cell. Enzyme structure comparison of CaGPI12 with Saccharomyces cerevisiae GPI12
-
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D102A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is active in absence of metal ions, but well stimulated by metal ions
D133A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is active in absence of metal ions, but well stimulated by metal ions
D45A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is active in absence of metal ions, but well stimulated by metal ions
D46A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is only slightly active in absence of metal ions and not stimulated by metal ions
D47A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is only slightly active in absence of metal ions, but well stimulated by metal ions
E79A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is active in absence of metal ions, but well stimulated by metal ions
H140A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is only slightly active in absence of metal ions and not stimulated by metal ions
H143A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is only slightly active in absence of metal ions, but well stimulated by metal ions
H43A
site-directed mutagenesis of the isolated cytoplasmic catalytic domain, the mutant is only slightly active in absence of metal ions, but well stimulated by metal ions
additional information
a CaGPI12 heterozygous is generated by disrupting one allele with HIS1 by a PCR-mediated approach using CaGPI12-HIS1 FP and CaGPI12-HIS1 RP by the lithium-acetate (LiAc) method. The CaGPI12 conditional null mutant is made by replacing its native promoter with MET3 promoter by using the pMET3-GFP-URA3 cassette. CaGPI12 is able to rescue the growth defect of the ScGPI12 conditional null strain as compared to the control strain carrying the YepHIS vector alone, suggesting that CaGPI12 functionally complements ScGPI12. Phenotype CaGPI12 and ScGPI12 conditional null strains, overview
additional information
-
a CaGPI12 heterozygous is generated by disrupting one allele with HIS1 by a PCR-mediated approach using CaGPI12-HIS1 FP and CaGPI12-HIS1 RP by the lithium-acetate (LiAc) method. The CaGPI12 conditional null mutant is made by replacing its native promoter with MET3 promoter by using the pMET3-GFP-URA3 cassette. CaGPI12 is able to rescue the growth defect of the ScGPI12 conditional null strain as compared to the control strain carrying the YepHIS vector alone, suggesting that CaGPI12 functionally complements ScGPI12. Phenotype CaGPI12 and ScGPI12 conditional null strains, overview
additional information
-
a CaGPI12 heterozygous is generated by disrupting one allele with HIS1 by a PCR-mediated approach using CaGPI12-HIS1 FP and CaGPI12-HIS1 RP by the lithium-acetate (LiAc) method. The CaGPI12 conditional null mutant is made by replacing its native promoter with MET3 promoter by using the pMET3-GFP-URA3 cassette. CaGPI12 is able to rescue the growth defect of the ScGPI12 conditional null strain as compared to the control strain carrying the YepHIS vector alone, suggesting that CaGPI12 functionally complements ScGPI12. Phenotype CaGPI12 and ScGPI12 conditional null strains, overview
-
additional information
comparison of secondary conformation of the mutant proteins, overview
additional information
-
comparison of secondary conformation of the mutant proteins, overview
additional information
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
additional information
-
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
additional information
-
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
-
additional information
-
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
-
additional information
-
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
-
additional information
-
two alleles of the GPI12 gene in Leishmania major are successfully removed enabling the generation of a null mutant, which supports the idea that GPI12 is not an essential gene for the growth and survival of Leishmania and the homozygous knockouts of Leishmania are able to survive. Generation of a mutant parasite that causes no damaged to the host
-
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Doering, T.L.; Masterson, W.J.; Englund, P.T.; Hart, G.W.
Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine
J. Biol. Chem.
264
11168-11173
1989
Trypanosoma sp.
brenda
Milne, K.G.; Field, R.A.; Masterson, W.J.; Cooaz, S.; Brimacombe, J.S.; Ferguson, M.A.J.
Partial purification and characterization of the N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol anchor biosynthesis in African trypanosomes
J. Biol. Chem.
269
16403-16408
1994
Trypanosoma sp.
brenda
Sharma, D.K.; Smith, T.K.; Crossman, A.; Brimacombe, J.S.; Ferguson, M.A.J.
Substrate specificity of the N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol membrane anchor biosynthesis in African trypanosomes and human cells
Biochem. J.
328
171-177
1997
Homo sapiens, Trypanosoma brucei
brenda
Smith, T.K.; Crossman, A.; Borissow, C.N.; Paterson, M.J.; Dix, A.; Brimacombe, J.S.; Ferguson, M.A.J.
Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors
EMBO J.
20
3322-3332
2001
Homo sapiens, Trypanosoma brucei
brenda
Smith, T.K.; Crossman, A.; Paterson, M.J.; Borissow, C.N.; Brimacombe, J.S.; Ferguson, M.A.J.
Specificities of enzymes of glycosylphosphatidylinositol biosynthesis in Trypanosoma brucei and HeLa Cells
J. Biol. Chem.
277
37147-37153
2002
Homo sapiens, Trypanosoma brucei
brenda
Pielsticker, L.K.; Mann, K.J.; Lin, W.L.; Sevlever, D.
Raft-like membrane domains contain enzymatic activities involved in the synthesis of mammalian glycosylphosphatidylinositol anchor intermediates
Biochem. Biophys. Res. Commun.
330
163-171
2005
Homo sapiens
brenda
Vats, D.; Vishwakarma, R.A.; Bhattacharya, S.; Bhattacharya, A.
Reduction of cell surface glycosylphosphatidylinositol conjugates in Entamoeba histolytica by antisense blocking of E. histolytica GlcNAc-phosphatidylinositol deacetylase expression: effect on cell proliferation, endocytosis, and adhesion to target cells
Infect. Immun.
73
8381-8392
2005
Entamoeba histolytica
brenda
Pottekat, A.; Menon, A.K.
Subcellular localization and targeting of N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the second enzyme in the glycosylphosphatidylinositol biosynthetic pathway
J. Biol. Chem.
279
15743-15751
2004
Homo sapiens (Q9Y2B2), Homo sapiens
brenda
Urbaniak, M.D.; Crossman, A.; Chang, T.; Smith, T.K.; van Aalten, D.M.; Ferguson, M.A.
The N-acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzyme
J. Biol. Chem.
280
22831-22838
2005
Rattus norvegicus (O35790), Trypanosoma brucei (Q382X3), Trypanosoma brucei
brenda
Shams-Eldin, H.; Azzouz, N.; Niehus, S.; Smith, T.K.; Schwarz, R.T.
An efficient method to express GPI-anchor proteins in insect cells
Biochem. Biophys. Res. Commun.
365
657-663
2008
Homo sapiens
brenda
Urbaniak, M.D.; Crossman, A.; Ferguson, M.A.
Probing Trypanosoma brucei glycosylphosphatidylinositol biosynthesis using novel precursor-analogues
Chem. Biol. Drug Des.
72
127-132
2008
Trypanosoma brucei
brenda
Abdelwahab, N.Z.; Urbaniak, M.D.; Ferguson, M.A.; Crossman, A.T.
Synthesis of potential metal-binding group compounds to examine the zinc dependency of the GPI de-N-acetylase metalloenzyme in Trypanosoma brucei
Carbohydr. Res.
346
708-714
2011
Trypanosoma brucei
brenda
Abdelwahab, N.Z.; Crossman, A.T.; Sullivan, L.; Ferguson, M.A.; Urbaniak, M.D.
Inhibitors incorporating zinc-binding groups target the GlcNAc-PI de-N-acetylase in Trypanosoma brucei, the causative agent of African sleeping sickness
Chem. Biol. Drug Des.
79
270-278
2012
Trypanosoma brucei
brenda
Ashraf, M.; Yadav, B.; Perinthottathil, S.; Kumar, K.S.; Vats, D.; Muthuswami, R.; Komath, S.S.
N-Acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase from Entamoeba histolytica: metal alters catalytic rates but not substrate affinity
J. Biol. Chem.
286
2543-2549
2011
Entamoeba histolytica
brenda
Urbaniak, M.D.; Capes, A.S.; Crossman, A.; ONeill, S.; Thompson, S.; Gilbert, I.H.; Ferguson, M.A.
Fragment screening reveals salicylic hydroxamic acid as an inhibitor of Trypanosoma brucei GPI GlcNAc-PI de-N-acetylase
Carbohydr. Res.
387
54-58
2014
Trypanosoma brucei, Trypanosoma brucei MITat1.4
brenda
Ashraf, M.; Sreejith, P.; Yadav, U.; Komath, S.S.
Catalysis by N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase (PIG-L) from Entamoeba histolytica: new roles for conserved residues
J. Biol. Chem.
288
7590-7595
2013
Entamoeba histolytica (C4M0W5), Entamoeba histolytica
brenda
Capes, A.S.; Crossman, A.; Urbaniak, M.D.; Gilbert, S.H.; Ferguson, M.A.; Gilbert, I.H.
Probing the substrate specificity of Trypanosoma brucei GlcNAc-PI de-N-acetylase with synthetic substrate analogues
Org. Biomol. Chem.
12
1919-1934
2014
Trypanosoma brucei
brenda
Almani, P.G.N.; Sharifi, I.; Kazemi, B.; Babaei, Z.; Bandehpour, M.; Salari, S.; Dezaki, E.S.; Tohidi, F.; Mohammadi, M.A.
The role of GlcNAc-PI-de-N-acetylase gene by gene knockout throughhomologous recombination and its consequences on survival, growthand infectivity of Leishmania major in in vitro and in vivo conditions
Acta Trop.
154
63-72
2016
Leishmania major (Q8I8A4), Leishmania major, Leishmania major 75 (Q8I8A4), Leishmania major IR (Q8I8A4), Leishmania major ER (Q8I8A4), Leishmania major MRHO (Q8I8A4)
brenda
Rashmi, M.; Swati, D.
In silico drug re-purposing against African sleeping sickness using GlcNAc-PI de-N-acetylase as an experimental target
Comput. Biol. Chem.
59
87-94
2015
Trypanosoma brucei (Q8I8A5), Trypanosoma brucei
brenda
Yadav, U.; Rai, K.T.; Sethi, S.C.; Chandraker, A.; Khan, M.A.; Komath, S.S.
Characterising N-acetylglucosaminylphosphatidylinositol de-N-acetylase (CaGpi12), the enzyme that catalyses the second step of GPI biosynthesis in Candida albicans
FEMS Yeast Res.
18
foy067
2018
Candida albicans (A0A1D8PEU2), Candida albicans, Candida albicans ATCC MYA-2876 (A0A1D8PEU2)
brenda