N-acetylglucosaminylphosphatidylinositol deacetylase

Thus, the two substrates of this enzyme are 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol and H₂O, whereas its two products are 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol and acetate.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase. Other names in common use include N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase, N-acetylglucosaminylphosphatidylinositol de-N-acetylase, GlcNAc-PI de-N-acetylase, GlcNAc-PI deacetylase, and acetylglucosaminylphosphatidylinositol deacetylase. This enzyme participates in 3 metabolic pathways: glycosylphosphatidylinositol(gpi)-anchor, and glycan structures - biosynthesis 2.

References

Doering TL, Masterson WJ, Englund PT, Hart GW (1989). "Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine". J. Biol. Chem. 264 (19): 11168–73. PMID 2525555.
Nakamura, N; Inoue, N; Watanabe, R; Takahashi, M; Takeda, J; Stevens, VL; Kinoshita, T (1997). "Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase". J. Biol. Chem. 272 (25): 15834–40. doi:10.1074/jbc.272.25.15834. PMID 9188481.
Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T. "Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis". Biochem. J. 339: 185–92. doi:10.1042/0264-6021:3390185. PMC 1220143. PMID 10085243.
Smit TK; Crossman, A; Borissow, CN; Paterson, MJ; Dix, A; Brimacombe, JS; Ferguson, MA (2001). "Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors". EMBO J. 20 (13): 3322–32. doi:10.1093/emboj/20.13.3322. PMC 125529. PMID 11432820.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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