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evolution
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sequence alignment reveals that the Trypanosoma brucei enzyme is far removed from the metazoan GnTI family and suggests that the parasite has adapted the beta3-glycosyltransferase family to catalyze beta1-2 linkages. It belongs to a family of putative UDP-sugar-dependent glycosyltransferases with similarity to the mammalian beta1-3-glycosyltransferase family. Enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
evolution
the modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms
evolution
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sequence alignment reveals that the Trypanosoma brucei enzyme is far removed from the metazoan GnTI family and suggests that the parasite has adapted the beta3-glycosyltransferase family to catalyze beta1-2 linkages. It belongs to a family of putative UDP-sugar-dependent glycosyltransferases with similarity to the mammalian beta1-3-glycosyltransferase family. Enzyme TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triantennary Man5GlcNAc2, which is the preferred substrate for metazoan enzymes
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malfunction
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Mgat1-null flies are viable but exhibit pronounced defects in locomotion. Neuron-specific RNAi knockdown of Mgat1 in wild-type flies results in locomotory defects, reduced life span, and about 50% reduction in enzyme activity
malfunction
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Mgat1-null mouse embryos die at 9.5-10.5 days after fertilization
malfunction
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modulating N-acetylglucosaminyltransferase I activity in cells can influence antibody effector functions
malfunction
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worms with either deletion or RNA-mediated down-regulation of the gly-14 gene are completely resistant to killing by bacteria on PGS medium
malfunction
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the bloodstream-form TbGT11 null mutant exhibits significantly modified protein N-glycans but normal growth in vitro and infectivity to rodents
malfunction
downregulation of MGAT1 inhibits glioma cell proliferation and migration, overview. Glut1 protein expression is significantly decreased in MGAT1 knockdown cells, but there is no significant change in Glut3. Activation of EGFR signalling by HB-EGF can rescue the inhibitory effects of MGAT1 knockdown on the expression of Glut1, but downregulation of MGAT1 does not significantly change the level of Glut1 mRNA. Downregulation of MGAT1 decreases the complex N-glycan of Glut1. Ectopic expression of Glut1 rescues the inhibitory effects of MGAT1 knockdown on glioma cell proliferation and migration
malfunction
enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Arabidopsis thaliana exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
malfunction
enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Phaeodactylum tricornutum exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus
malfunction
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the bloodstream-form TbGT11 null mutant exhibits significantly modified protein N-glycans but normal growth in vitro and infectivity to rodents
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metabolism
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part of N-glycan pathway
metabolism
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the enzyme controls the synthesis of paucimannose N-glycans
metabolism
the enzyme is involved in the N-glycan-branching pathway, overview. Regulation of cellular metabolite levels by Mgat1, overview
metabolism
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the first step in hybrid and complex N-glycan biosynthesis is initiated by N-acetylglucosaminyltransferase I (GnTI) through the addition of an N-acetylglucosamine (GlcNAc) residue to the alpha1-3-linked core mannose of Man5GlcNAc2
metabolism
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate
metabolism
eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate
metabolism
the N-glycomic repertoire of Caenorhabditis exhibits a large degree of plasticity even in the absence of key glycan processing enzymes from the Golgi apparatus
metabolism
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the first step in hybrid and complex N-glycan biosynthesis is initiated by N-acetylglucosaminyltransferase I (GnTI) through the addition of an N-acetylglucosamine (GlcNAc) residue to the alpha1-3-linked core mannose of Man5GlcNAc2
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physiological function
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N-glycan formation on glycoproteins
physiological function
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N-glycan formation on glycoproteins
physiological function
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plant N-glycan processing
physiological function
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enzyme-dependent N-glycans are essential for cell-cell and cell-matrix interactions
physiological function
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Mgat1-dependent N-glycans are required for normal development
physiological function
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Mgat1-dependent N-glycans are required for normal development
physiological function
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Mgat1-dependent N-glycans are required for normal development
physiological function
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in contrast to multicellular organisms, where the enzyme activity is essential for biosynthesis of both complex and hybrid N-glycans, Trypanosoma brucei TbGT11 null mutants produce atypical pseudohybrid glycans, indicating that the enzyme activity is not dependent on prior TbGnTI action. The enzyme GnTI reaction is essential for biosynthesis of both complex and hybridN-glycans. TbGnTII activity is not dependent on prior TbGnTI action
physiological function
AtGnTI (At4g38240) encodes for a Golgi enzyme that is responsible for the transfer of a terminal GlcNAc residue onto Man5GlcNAc2 N-glycan
physiological function
N-acetylglucosaminyltransferase I (MGAT1) is responsible for the conversion of high-mannose to hybrid and complex N-glycans. It promotes glioma cell proliferation and migration through increasing the stability of the glucose transporter GLUT1, MGAT1 interacted with Glut1 in U-87/MG cells, mechanism of MGAT1 promoting glioma cell proliferation, overview. MGAT1 regulates Glut1 N-glycosylation
physiological function
PtGnTI restores in vivo the biosynthesis of complex-type N-glycans in CHO Lec1 mutant that lacks endogenous GnTI activity
physiological function
the modification in the Golgi of N-glycans is catalyzed by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1). The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans
physiological function
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in contrast to multicellular organisms, where the enzyme activity is essential for biosynthesis of both complex and hybrid N-glycans, Trypanosoma brucei TbGT11 null mutants produce atypical pseudohybrid glycans, indicating that the enzyme activity is not dependent on prior TbGnTI action. The enzyme GnTI reaction is essential for biosynthesis of both complex and hybridN-glycans. TbGnTII activity is not dependent on prior TbGnTI action
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additional information
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steady-state distribution of the enzyme in the cis/medial-Golgi in plants is a prerequisite for efficient N-glycan processing in vivo
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
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analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview
additional information
Glut1 N-glycan structure is evaluated by N-glycosidase digestion. Glut1 in U87/MG cells is sensitive to PNGase F but resistant to endo H digestion, suggesting that the type of Glut1 N-glycan in U87/MG cells are mainly complex type N-glycan