2.4.1.132: GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
This is an abbreviated version!
For detailed information about GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.132
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2.4.1.132
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alpha-1,2-mannosyltransferase
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lipid-linked
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alpha-1,3-linked
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mannoses
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beta-glcnac
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oligosaccharide-lipids
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mannans
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pharmacology
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medicine
- 2.4.1.132
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alpha-1,2-mannosyltransferase
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lipid-linked
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alpha-1,3-linked
- mannoses
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beta-glcnac
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oligosaccharide-lipids
- mannans
- pharmacology
- medicine
Reaction
Synonyms
Alg2, Alg2 mannosyltransferase, Alg2 MTase, alpha-1,3-mannosyltransferase, alpha-1,3-ManT, asparagine-linked glycosylation 2, GDP-Man:Dol-PP-GlcNAc2Man2 alpha-1,3-mannosyltransferase, GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-oligosaccharide-lipid mannosyltransferase II, hALG2, mannosyltransferase II, mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid II, More, MTase, scAlg2, WfcD
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General Information
General Information on EC 2.4.1.132 - GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase
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malfunction
metabolism
physiological function
additional information
deficiency of GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase, is the cause of a congenital disorders of glycosylation designated CDG-Ii. The patients are normal at birth but develop in the 1st year of life a multisystemic disorder with mental retardation, seizures, coloboma of the iris, hypomyelination, hepatomegaly, and coagulation abnormalities. An accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol is observed in skin fibroblasts of the patient. Incubation of patient fibroblast extracts with Man1GlcNAc2-PP-dolichol and GDP-mannose reveals a severely reduced activity of the mannosyltransferase elongating Man1GlcNAc2-PP dolichol
malfunction
enzyme mutations are linked to congenital myasthenic syndrome
malfunction
loss of Alg2 promotes osteoblast differentiation in ST-2 cells without affecting the protein level of Runx2. Alg2 knockdown does not affect endoplasmic reticulum stress or bone morphogenetic protein, BMP, signaling in ST-2 cells. Atf4,also known as CCAAT/enhancer-binding protein homologous protein (Chop), is mildly upregulated by sAlg2, but only in BMP-2-treated cells. The expression of a target of the Atf6 pathway, heat shock protein 5 (Hspa5), is not altered by loss of Alg2
malfunction
cells deleted for ALG2 are inviable. Mutant alg2 alleles display intraallelic complementation
malfunction
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loss of Alg2 promotes osteoblast differentiation in ST-2 cells without affecting the protein level of Runx2. Alg2 knockdown does not affect endoplasmic reticulum stress or bone morphogenetic protein, BMP, signaling in ST-2 cells. Atf4,also known as CCAAT/enhancer-binding protein homologous protein (Chop), is mildly upregulated by sAlg2, but only in BMP-2-treated cells. The expression of a target of the Atf6 pathway, heat shock protein 5 (Hspa5), is not altered by loss of Alg2
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malfunction
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cells deleted for ALG2 are inviable. Mutant alg2 alleles display intraallelic complementation
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ALG2 is an alpha-1,3-mannosyltransferase that catalyses the second and third mannosylation steps in the N-linked glycosylation pathway
metabolism
ALG2 is an alpha-1,3-mannosyltransferase that catalyses the second and third mannosylation steps in the N-linked glycosylation pathway
metabolism
asparagine-linked glycosylation (ALG) is one of the most common protein modification reactions in eukaryotic cells, as many proteins that are translocated across or integrated into the rough endoplasmic reticulum carry N-linked oligosaccharides. Linkage between an asparagine-linked glycosylation mannosyltransferase gene and osteochondrogenesis
metabolism
the fourth and fifth steps of lipid-linked oligosaccharide (LLO) synthesis are catalyzed by Alg2, an unusual mannosyltransferase (MTase) with two different MTase activities
metabolism
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asparagine-linked glycosylation (ALG) is one of the most common protein modification reactions in eukaryotic cells, as many proteins that are translocated across or integrated into the rough endoplasmic reticulum carry N-linked oligosaccharides. Linkage between an asparagine-linked glycosylation mannosyltransferase gene and osteochondrogenesis
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metabolism
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the fourth and fifth steps of lipid-linked oligosaccharide (LLO) synthesis are catalyzed by Alg2, an unusual mannosyltransferase (MTase) with two different MTase activities
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human immunodeficiency virus type 1 enhancer-binding protein 3, Hivep3 or Schnurri-3, Zas3, and Krc, is essential for the expression of asparagine-linked glycosylation 2 in the regulation of osteoblast and chondrocyte differentiation. Alg2 suppresses osteoblast differentiation by inhibiting the activity of Runx2. Alg2 silencing suppresses the expression of Creb3l2 and chondrogenesis. Enzyme ALG2 is associated with osteochondrogenesis, Alg2 is a downstream mediator of Hivep3 and suppresses osteogenesis, whereas it promotes chondrogenesis. Regulation analysis, overview
physiological function
the enzyme transfers D-mannosyl units to endoplasmic reticulum membrane-bound N-acetylglucosaminyl dolichyl-phosphates
physiological function
the enzyme transfers D-mannosyl units to endoplasmic reticulum membrane-bound N-acetylglucosaminyl dolichyl-phosphates
physiological function
asparagine (N)-linked glycosylation requires the ordered, stepwise synthesis of lipid-linked oligosaccharide (LLO) precursor Glc3Man9GlcNAc2-diphosphate-dolichol (Glc3Man9Gn2-PDol) on the endoplasmic reticulum. The fourth and fifth steps of LLO synthesis are catalyzed by Alg2, an unusual mannosyltransferase (MTase) with two different MTase activities. Alg2 adds both an alpha1,3- and alpha1,6-mannose ontoManGlcNAc2-PDol to form the trimannosyl core Man3GlcNAc2-PDol. Alg2-dependent Man3GlcNAc2-PDol production relies on net-neutral lipids with a propensity to form bilayers
physiological function
WfcD is the first characterized bacterial mannosyltransferase that acts on the Man-alpha-(1->3)-GlcNAc linkage
physiological function
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human immunodeficiency virus type 1 enhancer-binding protein 3, Hivep3 or Schnurri-3, Zas3, and Krc, is essential for the expression of asparagine-linked glycosylation 2 in the regulation of osteoblast and chondrocyte differentiation. Alg2 suppresses osteoblast differentiation by inhibiting the activity of Runx2. Alg2 silencing suppresses the expression of Creb3l2 and chondrogenesis. Enzyme ALG2 is associated with osteochondrogenesis, Alg2 is a downstream mediator of Hivep3 and suppresses osteogenesis, whereas it promotes chondrogenesis. Regulation analysis, overview
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physiological function
Escherichia coli O141
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WfcD is the first characterized bacterial mannosyltransferase that acts on the Man-alpha-(1->3)-GlcNAc linkage
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physiological function
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asparagine (N)-linked glycosylation requires the ordered, stepwise synthesis of lipid-linked oligosaccharide (LLO) precursor Glc3Man9GlcNAc2-diphosphate-dolichol (Glc3Man9Gn2-PDol) on the endoplasmic reticulum. The fourth and fifth steps of LLO synthesis are catalyzed by Alg2, an unusual mannosyltransferase (MTase) with two different MTase activities. Alg2 adds both an alpha1,3- and alpha1,6-mannose ontoManGlcNAc2-PDol to form the trimannosyl core Man3GlcNAc2-PDol. Alg2-dependent Man3GlcNAc2-PDol production relies on net-neutral lipids with a propensity to form bilayers
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the conserved C-terminal EX7E motif, N-terminal cytosolic tail, and 3G-rich loop motifs in Alg2 play crucial roles for these activities, both in vitro and in vivo. Alg2 immunoprecipitates from extracts of yeast microsomal membranes also displays both alpha1,3- and alpha1,6-mannosyltransferase (MTase) activities. The conserved Val62 residue is required for yeast Alg2 function. The first E (E335) and His-336 are partially required for alpha1,6-mannosylation, and importance of both E335 and E343 of the EX7E domain for Alg2 function in vivo. Identification of three conserved G-rich motifs in scAlg2, located in the N-terminal cytosolic short tail, in the middle of Alg2, and in the C-terminal domain. Residues G17, G19, and G20 are within the N-terminal cytosolic tail of Alg2, importance of this domain for Alg2 function
additional information
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the conserved C-terminal EX7E motif, N-terminal cytosolic tail, and 3G-rich loop motifs in Alg2 play crucial roles for these activities, both in vitro and in vivo. Alg2 immunoprecipitates from extracts of yeast microsomal membranes also displays both alpha1,3- and alpha1,6-mannosyltransferase (MTase) activities. The conserved Val62 residue is required for yeast Alg2 function. The first E (E335) and His-336 are partially required for alpha1,6-mannosylation, and importance of both E335 and E343 of the EX7E domain for Alg2 function in vivo. Identification of three conserved G-rich motifs in scAlg2, located in the N-terminal cytosolic short tail, in the middle of Alg2, and in the C-terminal domain. Residues G17, G19, and G20 are within the N-terminal cytosolic tail of Alg2, importance of this domain for Alg2 function
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