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Literature summary extracted from

  • 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 (2018), FEMS Yeast Res., 18, foy067 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.89 gene CaGPI12 is a single copy of the gene on chromosome 1 Candida albicans

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.89 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 Candida albicans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.89 EDTA complete inhibition at 10 mM, the enzyme irreversibly loses activity upon incubation with a metal chelator Candida albicans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.89 membrane the enzyme sequence contains three short hydrophobic transmembrane stretches, one at the N-terminus and two at the C-terminus Candida albicans 16020
-
3.5.1.89 microsome
-
 Candida albicans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.89 Ca2+ stimulates Candida albicans
3.5.1.89 Co2+ stimulates Candida albicans
3.5.1.89 Mg2+ stimulates Candida albicans
3.5.1.89 Mn2+ stimulates Candida albicans
3.5.1.89 additional information a metal-dependent enzyme that is stimulated by divalent cations but shows no preference for Zn2+ unlike the mammalian homologue. It irreversibly loses activity upon incubation with a metal chelator. Fe2+ has no significant effect on the enzyme activity Candida albicans
3.5.1.89 Zn2+ required, does not activate the enzyme, a metal-dependent enzyme Candida albicans

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 Candida albicans
-
 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 Candida albicans ATCC MYA-2876
-
 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.89 Candida albicans A0A1D8PEU2
-
-
3.5.1.89 Candida albicans ATCC MYA-2876 A0A1D8PEU2
-
-

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
-
 Candida albicans 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 the substrate is prepared from Saccharomyces cerevisiae microsomes. [6-3H]GlcN-PI is converted to [6-3H]GlcNAc-PI using anhydride Candida albicans 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
-
 Candida albicans ATCC MYA-2876 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 the substrate is prepared from Saccharomyces cerevisiae microsomes. [6-3H]GlcN-PI is converted to [6-3H]GlcNAc-PI using anhydride Candida albicans ATCC MYA-2876 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
-
 ?
3.5.1.89 additional information the enzyme shows an overall low activity Candida albicans ?
-
-
3.5.1.89 additional information the enzyme shows an overall low activity Candida albicans ATCC MYA-2876 ?
-
-

Subunits

EC Number Subunits Comment Organism
3.5.1.89 ? x * 42000, about, sequence calculation Candida albicans

Synonyms

EC Number Synonyms Comment Organism
3.5.1.89 CaGpi12
-
 Candida albicans
3.5.1.89 GPI12
-
 Candida albicans
3.5.1.89 N-Acetylglucosaminylphosphatidylinositol de-N-acetylase
-
 Candida albicans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.89 30
-
-
 Candida albicans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.89 7.5
-
-
 Candida albicans

General Information

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