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Literature summary for 3.5.1.89 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

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

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons Trypanosoma brucei

Inhibitors

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

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

Natural Substrates/ Products (Substrates)

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
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6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
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?

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei Q8I8A5
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O
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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

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

Synonyms

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

General Information

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