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Literature summary extracted from

  • Rashmi, M.; Swati, D.
    In silico drug re-purposing against African sleeping sickness using GlcNAc-PI de-N-acetylase as an experimental target (2015), Comput. Biol. Chem., 59, 87-94 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.89 drug development the enzyme is a target in the treatment of African sleeping sickness Trypanosoma brucei

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.89 sequence comparisons Trypanosoma brucei

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.89 ethambutol docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness Trypanosoma brucei
3.5.1.89 metaraminol docking study, the effective enzyme inhibitor may be useful in the treatment of African sleeping sickness Trypanosoma brucei
3.5.1.89 additional information inhibitor search by structural based virtual screening (SBVS), molecular modeling, and docking study, overview Trypanosoma brucei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.89 Zn2+ enzyme contains a zinc binding site, Zn2+ docking Trypanosoma brucei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.89 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

EC Number Organism UniProt Comment Textmining
3.5.1.89 Trypanosoma brucei Q8I8A5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.89 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
-
 Trypanosoma brucei 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
 ?
3.5.1.89 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

EC Number Subunits Comment Organism
3.5.1.89 More domain determination and protein structure homology modelling using ten templates by different threading programs Trypanosoma brucei

Synonyms

EC Number Synonyms Comment Organism
3.5.1.89 GlcNAc-PI de-N-acetylase
-
 Trypanosoma brucei
3.5.1.89 GPI12
-
 Trypanosoma brucei

General Information

EC Number General Information Comment Organism
3.5.1.89 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
3.5.1.89 metabolism the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Trypanosoma brucei Trypanosoma brucei
3.5.1.89 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
3.5.1.89 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