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4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
alpha-D-mannose + Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 28.8% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
GDP-mannose + alpha-1,6-D-mannobiose
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two distinct Mnn9p-containing multi-protein complexes add multiple mannosyl residues forming a series of poly-mannose structures in vitro, no substrate of Och1p
formation of a series of poly-mannose structures, which contain mainly alpha-1,6- and some additional alpha-1,2-linked mannoses
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GDP-mannose + Man8GlcNAc
GDP + Man9GlcNAc
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Man8GlcNAc from thyroglobulin Man9GlcNAc by treatment with yeast specific mannosidase, specificity, enzyme catalyzes addition of mannose to the alpha-1,3-mannose of the substrate, initiates outer chain formation
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?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
GDP-mannose + Man9GlcNAc
GDP + Man10GlcNAc
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Man9GlcNAc from thyroglobulin, specificity, enzyme catalyzes addition of mannose to the alpha-1,3-mannose of the substrate, initiates outer chain formation
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GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
GDP-mannose + Manalpha(1,2)Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 74.2% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine. Och1p has the catalytic potential to transfer two molecules of mannose to Manalpha(1,2)Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine. The second mannose is attached with alpha1,6-linkage to either the alpha1,6-linked or the alpha1,3-linked mannose that is attached to alpha1,6-linked mannose
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GDP-mannose + Manalpha(1,2)Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 58.5% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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?
GDP-mannose + Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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GDP-mannose + Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 66.1% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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?
GDP-mannose + Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 28.8% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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?
GDP-mannose + Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 14.4% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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?
GDP-mannose + Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GlcNAcbeta(1,4)GlcNAc-pyridylamine
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recombinant enzyme shows 14.4% of the activity with Manalpha(1,2)Manalpha(1,6)[Manalpha(1,3)]Manalpha(1,6)[Manalpha(1,2)Manalpha(1,2)Manalpha(1,3)]Manbeta(1,4)GLcNAcbeta(1,4)GlcNAc-pyridylamine
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?
GDP-mannose + Manalpha(1-2)Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
GDP + Manalpha(1-2)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
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Man9GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate, removal of the alpha-1,2-linked mannose residue from Man9GlcNAc is not essential for enzyme activity
Man10GlcNAc
?
GDP-mannose + Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
GDP + Manalpha(1-2)[Manalpha(1-6)]Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc
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Man8GlcNAc from rat liver glycoproteins and thyroglobulin, enzyme initiates outer chain synthesis, the mannose residue added is alpha-1,6-linked to the alpha-1,6-mannose residue of the substrate
Man9GlcNAc
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GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
GDP-mannose + oligosaccharide acceptor
?
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Mnn9p is involved in protein mannosylation, incorporates alpha-1,6-linked mannose residues, the elongation of the N-glycan outer chain, initiated by Och1p, is continued by two mannosyltransferase complexes: V-complex composed of Mnn9p and Van1p and A-complex composed of Mnn9p, Anp1p, Hoc1p, Mnn10p and Mnn11p
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GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
GDP-mannose + pyridylaminated Man5GlcNAc2
GDP + pyridylaminated Man6GlcNAc2
incorporates alpha-1,6-linked mannose, poor substrate
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GDP-mannose + pyridylaminated Man6GlcNAc2
GDP + pyridylaminated Man7GlcNAc2
incorporates alpha-1,6-linked mannose
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GDP-mannose + pyridylaminated Man7GlcNAc2
GDP + pyridylaminated Man8GlcNAc2
incorporates alpha-1,6-linked mannose
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GDP-mannose + pyridylaminated Man8GlcNAc2
GDP + pyridylaminated Man9GlcNAc2
incorporates alpha-1,6-linked mannose
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GDP-mannose + pyridylaminated Man9GlcNAc2
GDP + pyridylaminated Man10GlcNAc2
incorporates alpha-1,6-linked mannose
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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GDP-mannose + pyridylaminated oligosaccharide acceptor
GDP + pyridylaminated alpha-mannosyl-1,6-oligosaccharide
incorporates alpha-1,6-linked mannose, substrate specificity
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GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
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additional information
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4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
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4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
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GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
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GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
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?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
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best acceptor for Och1p, initiation-specific alpha-1,6-mannosyltransferase that requires the intact structure of Man8GlcNAc for efficient mannose outer chain initiation
additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
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GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
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best acceptor for Och1p, initiation-specific alpha-1,6-mannosyltransferase that requires the intact structure of Man8GlcNAc for efficient mannose outer chain initiation
additional Man is attached with an alpha-1,6-linkage at the site where mannose outer chain elongation initiates
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GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
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enzyme incorporates alpha-1,6-linked mannose into the substrate
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GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
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enzyme incorporates alpha-1,6-linked mannose into the substrate
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?
GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
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mannopentaose from Candida albicans, substrate specificity study, structural requirement of enzyme is Manalpha(1-3)Manalpha(1-)
structure, presence of an alpha-1,6 branching mannose unit
?
GDP-mannose + Manalpha(1-3)Manalpha(1-2)Manalpha(1-3)Manalpha(1-2)Man
GDP + Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-2)Manalpha(1-2)Manalpha(1-2)Man
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mannopentaose from Candida albicans, substrate specificity study, structural requirement of enzyme is Manalpha(1-3)Manalpha(1-)
structure, presence of an alpha-1,6 branching mannose unit
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Mnn9p incorporates alpha-1,6-linked mannose residues, the elongation of the N-glycan outer chain, initiated by Och1p, is continued by two mannosyltransferase complexes: V-complex composed of Mnn9p and Van1p and A-complex composed of Mnn9p, Anp1p, Hoc1p, Mnn10p and Mnn11p, study of the interactions between the subunits of the mannosyltransferase complexes
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?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Mnn9p is a component of two distinct multi-protein complexes, both having alpha-1,6-mannosyltransferase activity: a complex of Mnn9p and Van1p and a complex of Mnn9p, Anp1p, Mnn10p, Mnn11p and Hoc1p
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GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
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Mnn9p is associated in two distinct multi-protein complexes, both having alpha-1,6-mannosyltransferase activity, they add multiple mannosyl residues forming hypermannose structures, Och1p adds the initiating alpha-1,6-mannose residue to an N-linked Man8GlcNAc2 structure, the Mnn9p-containing protein complexes add further alpha-1,6-mannose residues synthesizing the backbone of the outer chain of N-linked glycans
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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substrate specificity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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various high mannose-type oligosaccharides as acceptors, Man8GlcNAc2-PA is the best acceptor, the loss of 1 or 2 alpha-1,2-mannoses from Man8GlcNAc2 reduces the activity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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substrate specificity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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various high mannose-type oligosaccharides as acceptors, Man8GlcNAc2-PA is the best acceptor, the loss of 1 or 2 alpha-1,2-mannoses from Man8GlcNAc2 reduces the activity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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substrate specificity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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SpOch1p
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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substrate specificity
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GDP-mannose + pyridylaminated oligosaccharide acceptor
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SpOch1p
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GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
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substrate for activity assay
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GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
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substrate for activity assay
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additional information
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enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
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additional information
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transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
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additional information
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transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
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additional information
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enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
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additional information
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the enzyme is required for cell-wall organization and proper functioning of the secretory pathway
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additional information
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HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
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additional information
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HpOCH1 is the key enzyme responsible for initiating N-linked outer chain biosynthesis by adding the first alpha-1,6-mannose residue onto the core oligosaccharide
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additional information
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no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
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additional information
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Mnn9p, no acceptor: alpha-1,2-mannobiose
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additional information
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Och1p adds one alpha-1,6-linked mannose residue to the core glycan of glycoproteins, e.g. pro-carboxypeptidase Y, the soluble cell wall protein Scw4p
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additional information
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enzyme initiates outer chain formation of oligosaccharides
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additional information
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Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
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additional information
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Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
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additional information
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OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
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additional information
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involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins
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additional information
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Och1p is essential for the outer chain elongation of N-linked oligosaccharides
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additional information
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Mnn9p is involved in the formation of mannan chains in the Golgi
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additional information
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Och1p is responsible for starting the extension of the primary N-glycans in the Golgi by addition of an alpha-1,6-mannose residue to the core glycan of glycoproteins
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additional information
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two distinct Mnn9p-containing multi-protein complexes are responsible for the synthesis and initial branching of the long alpha-1,6-linked backbone of the hypermannose structure attached to many yeast glycoproteins, the long alpha-1,6-linked backbone is attached to an initial alpha-1,6-mannose residue transferred to the core structure by Och1p
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additional information
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the N-linked oligosaccharide modification in the Golgi apparatus is initiated by alpha1,6-mannosyltransferase (encoded by the OCH1 gene) with the addition of mannose to the Man8GlcNAc2 or Man9GlcNAc2 endoplasmic reticulum intermediates
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additional information
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Och1p has the potential to transfer two mannoses from GDP-mannose
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additional information
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transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
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additional information
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both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
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additional information
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both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
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additional information
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Mnn9p is required for the addition of the long alpha-1,6-mannose backbone of the complex mannan and for the complex glycosylation of secreted proteins
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additional information
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both the presence and the priming activity of enzyme ScMnn9 are required for the formation of the alpha-1,6-mannose backbone of mannan proteins. Determination of the structure of the mannosyltransferase domain of ScMnn9 in complex with manganese and GDP, overview. Development of a coupled enzyme assay that involves Bacillus subtilis TN-31 aman6 (Aman6), an alpha-1,6-mannosidase, as only one additional enzyme, in contrast to the established glycosyltransferase assays where the release of GDP is measured by NADH oxidation through pyruvate kinase and lactate dehydrogenase
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additional information
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Och1p is functional in the initiation of alpha-1,6-polymannose outer chain addition to the N-linked core oligosaccharide in yeast, Man5GlcNAc2 and Man8GlcNAc2
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additional information
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OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
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additional information
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no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
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additional information
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Och1p is essential for the outer chain elongation of N-linked oligosaccharides
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additional information
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SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
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additional information
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SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
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additional information
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enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
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additional information
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SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
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additional information
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SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
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additional information
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SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
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additional information
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enzyme is required for the initiation of outer chain elongation of N-linked oligosaccharides of cell wall mannoproteins, transcriptional control of the och1+ gene, gene expression is not regulated during the cell cycle, but is induced by salt stress through the transcription factor Atf1p
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additional information
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SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
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additional information
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involved in N-glycosylation pathway
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additional information
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transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
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?