N-acetylglucosaminylphosphatidylinositol deacetylase

N-acetylglucosaminylphosphatidylinositol deacetylase
Identifiers
EC number	3.5.1.89
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction

6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H₂O $\rightleftharpoons$ 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate

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. 
• Kinoshita T; 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 (Pt 1). "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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220143. 
• JS, Ferguson MA; 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125529. 

This hydrolase article is a stub. You can help Wikipedia by expanding it.v · Categories: EC 3.5.1 Enzymes of unknown structure Hydrolase stubs Wikimedia Foundation. 2010. Игры ⚽ Поможем сделать НИР Donald McKay (politician) The Dynamic Gallery of Thoughts Look at other dictionaries: List of EC numbers (EC 3) — This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 3.1: Acting on Ester BondsEC… …   Wikipedia Hydrolase — Cristal de lysozyme Les hydrolases constituent une classe d enzymes qui catalysent les réactions d hydrolyse de molécules suivant la réaction générale : R R + H2O ⇌ R OH + R H On y trouve par exemple les estérases, qui hydrolysent les …   Wikipédia en Français EC 3.5 — Le groupe EC3.5 rassemble des enzymes appartenant à la famille des hydrolases. Elles ont pour particularité de catalyser des réactions d hydrolyse dans des molécules possédant un carbone et un azote liés par liaison simple, double ou triple. À la …   Wikipédia en Français 18+ © Academic, 2000-2025 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”