Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target in the treatment of African sleeping sickness | Trypanosoma brucei |
Cloned (Comment) | Organism |
---|---|
sequence comparisons | Trypanosoma brucei |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ethambutol | docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness | Trypanosoma brucei | |
metaraminol | docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness | Trypanosoma brucei | |
additional information | inhibitor search by structural based virtual screening (SBVS), molecular modeling, and docking study, overview | Trypanosoma brucei |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | enzyme contains a zinc binding site, Zn2+ docking | Trypanosoma brucei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O | Trypanosoma brucei | - |
6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trypanosoma brucei | Q8I8A5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O | - |
Trypanosoma brucei | 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate | - |
? | |
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O | substrate binding analysis by docking with Zn2+ to the enzyme's active site | Trypanosoma brucei | 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | domain determination and protein structure homology modelling using ten templates by different threading programs | Trypanosoma brucei |
Synonyms | Comment | Organism |
---|---|---|
GlcNAc-PI de-N-acetylase | - |
Trypanosoma brucei |
GPI12 | - |
Trypanosoma brucei |
General Information | Comment | Organism |
---|---|---|
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 | Trypanosoma brucei |
metabolism | the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Trypanosoma brucei | Trypanosoma brucei |
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 | Trypanosoma brucei |
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 | Trypanosoma brucei |