EC Number   |
General Information |
Reference |
|---|
   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 |
756513 |
| 3.5.1.89 | 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 |
-, 755748 |
| 3.5.1.89 | 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 |
-, 756746 |
| 3.5.1.89 | metabolism |
the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Candida albicans |
-, 756746 |
| 3.5.1.89 | metabolism |
the enzyme catalyses the second step of glycosylphosphatidylinositol biosynthesis in Trypanosoma brucei |
756513 |
| 3.5.1.89 | 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 |
734251 |
| 3.5.1.89 | 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 |
734824 |
| 3.5.1.89 | more |
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 |
756513 |
| 3.5.1.89 | more |
residues Asp46 and His140 of the enzyme are important for catalysis |
734251 |
| 3.5.1.89 | more |
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 |
-, 756746 |
