Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
-
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
-
-
?
GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
GDP-mannose + alpha-1,6-D-mannobiose
?
-
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
?
GDP-mannose + Man8GlcNAc
GDP + Man9GlcNAc
-
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
-
?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
GDP-mannose + Man9GlcNAc
GDP + Man10GlcNAc
-
Man9GlcNAc from thyroglobulin, specificity, enzyme catalyzes addition of mannose to the alpha-1,3-mannose of the substrate, initiates outer chain formation
-
?
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
?
-
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
-
-
?
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
?
-
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
-
-
?
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
?
-
-
-
-
?
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
?
-
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
-
-
?
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
?
-
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
-
-
?
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
?
-
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
-
-
?
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
?
-
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
-
-
?
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
-
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
-
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
?
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
?
-
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
-
?
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
-
?
GDP-mannose + pyridylaminated Man6GlcNAc2
GDP + pyridylaminated Man7GlcNAc2
incorporates alpha-1,6-linked mannose
-
?
GDP-mannose + pyridylaminated Man7GlcNAc2
GDP + pyridylaminated Man8GlcNAc2
incorporates alpha-1,6-linked mannose
-
?
GDP-mannose + pyridylaminated Man8GlcNAc2
GDP + pyridylaminated Man9GlcNAc2
incorporates alpha-1,6-linked mannose
-
?
GDP-mannose + pyridylaminated Man9GlcNAc2
GDP + pyridylaminated Man10GlcNAc2
incorporates alpha-1,6-linked mannose
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
GDP + pyridylaminated alpha-mannosyl-1,6-oligosaccharide
incorporates alpha-1,6-linked mannose, substrate specificity
-
?
GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
?
additional information
?
-
4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
-
-
-
?
4-methylumbelliferyl-alpha-D-Man + GDP-mannose
4-methylumbelliferyl-alpha-D-Man-(1->6)-D-Man + GDP
-
-
-
?
GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
-
-
-
?
GDP-mannose + 6-O-alpha-D-mannopyranosyl-D-mannopyranose
GDP + alpha-(1->6)-D-mannotriose
-
-
-
?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
-
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
?
GDP-mannose + Man8GlcNAc2-PA
GDP + Man9GlcNAc2-PA
-
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
?
GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
-
enzyme incorporates alpha-1,6-linked mannose into the substrate
-
-
?
GDP-mannose + Man9GlcNAc2-PA
GDP + Man10GlcNAc2-PA
-
enzyme incorporates alpha-1,6-linked mannose into the substrate
-
-
?
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
-
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
-
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
-
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
-
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
-
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
-
?
GDP-mannose + oligosaccharide acceptor
GDP + alpha-mannosyl-1,6-oligosaccharide
-
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
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
substrate specificity
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
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
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
substrate specificity
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
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
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
substrate specificity
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
SpOch1p
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
substrate specificity
-
-
?
GDP-mannose + pyridylaminated oligosaccharide acceptor
?
-
SpOch1p
-
-
?
GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
?
-
substrate for activity assay
-
-
?
GDP-mannose + pyridylamino-Manalpha1-3Man-alpha1-2Manalpha1-2Manalpha1-2Man
?
-
substrate for activity assay
-
-
?
additional information
?
-
-
enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
-
enzyme also transfers the alpha-1,6-linked branching mannose unit to the mannan of Saccharomyces cerevisiae
-
-
?
additional information
?
-
-
the enzyme is required for cell-wall organization and proper functioning of the secretory pathway
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
-
-
?
additional information
?
-
-
Mnn9p, no acceptor: alpha-1,2-mannobiose
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
enzyme initiates outer chain formation of oligosaccharides
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
-
-
?
additional information
?
-
-
involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins
-
-
?
additional information
?
-
-
Och1p is essential for the outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
-
Mnn9p is involved in the formation of mannan chains in the Golgi
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Och1p has the potential to transfer two mannoses from GDP-mannose
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
-
-
?
additional information
?
-
-
no acceptors for Och1p: Man5GlcNAc2 completely lacking alpha-1,2-Man, Man8GlcNAcOH
-
-
?
additional information
?
-
-
Och1p is essential for the outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
-
?
additional information
?
-
-
SpOch1p has a wider substrate specificity than ScOch1p from Saccharomyces cerevisiae
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
-
?
additional information
?
-
-
SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in N-glycosylation pathway
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GDP-mannose + oligosaccharide acceptor
?
-
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
-
?
additional information
?
-
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
-
the enzyme is required for cell-wall organization and proper functioning of the secretory pathway
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme initiates outer chain formation of oligosaccharides
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
-
-
?
additional information
?
-
-
involved in glycoprotein biosynthesis, enzyme catalyzes the first step specific to N-linked oligosaccharide synthesis and the biosynthesis of the outer chain of mannoproteins
-
-
?
additional information
?
-
-
Och1p is essential for the outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
-
Mnn9p is involved in the formation of mannan chains in the Golgi
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
OCH1 gene encoded enzyme initiates the polymannose outer chain elongation of N-glycans, regulation of the OCH1 transcription
-
-
?
additional information
?
-
-
Och1p is essential for the outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
-
?
additional information
?
-
-
SpOch1p is a key enzyme in outer chain elongation of N-linked oligosaccharides on glycoproteins
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
SpOch1p is a key enzyme of outer chain elongation of N-linked oligosaccharides
-
-
?
additional information
?
-
-
involved in N-glycosylation pathway
-
-
?
additional information
?
-
-
transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1-6)-D-mannosyl-D-mannose linkage
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Yip, C.L.; Welch, S.K.; Klebl, F.; Gilbert, T.; Seidel, P.; Grant, F.; O'Hara, P.J.; MacKay, V.L.
Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins
Proc. Natl. Acad. Sci. USA
91
2723-2727
1994
Saccharomyces cerevisiae
brenda
Romero, P.A.; Herscovics, A.
Glycoprotein biosynthesis in Saccharomyces cerevisiae. Characterization of alpha-1,6-mannosyltransferase which initiates outer chain formation
J. Biol. Chem.
264
1946-1950
1989
Saccharomyces cerevisiae
brenda
Reason, A.J.; Dell, A.; Romero, P.A.; Herscovics, A.
Specificity of the mannosyltransferase which initiates outer chain formation in Saccharomyces cerevisiae
Glycobiology
1
387-391
1991
Saccharomyces cerevisiae
brenda
Nakanishi-Shindo, Y.; Nakayama, K.; Tanaka, A.; Toda, Y.; Jigami, Y.
Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae
J. Biol. Chem.
268
26338-26345
1993
Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Yamamoto, K.; Okamoto, M.; Yoko-o, T.; Jigami, Y.
Salt stress induces the expression of the Schizosaccharomyces pombe och1+, which encodes an initiation-specific alpha-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins
Biosci. Biotechnol. Biochem.
67
927-929
2003
Schizosaccharomyces pombe, Schizosaccharomyces pombe Och1p
brenda
Cui, Z.; Horecka, J.; Jigami, Y.
Cdc4 is involved in the transcriptional control of OCH1, a gene encoding alpha-1,6-mannosyltransferase in Saccharomyces cerevisiae
Yeast
19
69-77
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Tsukahara, K.; Watanabe, T.; Yokoo, T.; Chigami, Y.
Schizosaccharomyces pombe och1+ gene encoding alpha-1,6-mannosyltransferase and use of och1+ gene knockout fission yeast for production of glycoprteins with reduced glycosylation
Jpn. Kokai Tokkyo Koho
11pp
2001
Schizosaccharomyces pombe, Schizosaccharomyces pombe Och1p
-
brenda
Nakayama, K.; Nakanishi-Shindo, Y.; Tanaka, A.; Haga-Toda, Y.; Jigami, Y.
Substrate specificity of alpha-1,6-mannosyltransferase that initiates N-linked mannose outer chain elongation in Saccharomyces cerevisiae
FEBS Lett.
412
547-550
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae Och1p
brenda
Suzuki, A.; Shibata, N.; Suzuki, M.; Saitoh, F.; Takata, Y.; Oshie, A.; Oyamada, H.; Kobayashi, H.; Suzuki, S.; Okawa, Y.
Characterization of alpha-1,6-mannosyltransferase responsible for the synthesis of branched side chains in Candida albicans mannan
Eur. J. Biochem.
240
37-44
1996
Candida albicans, Candida albicans NIH B-792 serotype B
brenda
Kojima, H.; Hashimoto, H.; Yoda, K.
Interaction among the subunits of Golgi membrane mannosyltransferase complexes of the yeast Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
63
1970-1976
1999
Saccharomyces cerevisiae
brenda
Jungmann, J.; Munro, S.
Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with alpha-1,6-mannosyltransferase activity
EMBO J.
17
423-434
1998
Saccharomyces cerevisiae
brenda
Yoko-o, T.; Tsukahara, K.; Watanabe, T.; Hata-Sugi, N.; Yoshimatsu, K.; Nagasu, T.; Jigami, Y.
Schizosaccharomyces pombe och1+ encodes alpha-1,6-mannosyltransferase that is involved in outer chain elongation of N-linked oligosaccharides
FEBS Lett.
489
75-80
2001
Schizosaccharomyces pombe (Q9UTR6), Schizosaccharomyces pombe
brenda
Karhinen, L.; Makarow, M.
Activity of recycling Golgi mannosyltransferases in the yeast endoplasmic reticulum
J. Cell Sci.
117
351-358
2004
Saccharomyces cerevisiae
brenda
Todorow, Z.; Spang, A.; Carmack, E.; Yates, J.; Schekman, R.
Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum
Proc. Natl. Acad. Sci. USA
97
13643-13648
2000
Saccharomyces cerevisiae
brenda
Barnay-Verdier, S.; Boisrame, A.; Beckerich, J.M.
Identification and characterization of two alpha-1,6-mannosyltransferases, Anl1p and Och1p, in the yeast Yarrowia lipolytica
Microbiology
150
2185-2195
2004
Yarrowia lipolytica
brenda
Kitajima, T.; Chiba, Y.; Jigami, Y.
Saccharomyces cerevisiae alpha1,6-mannosyltransferase has a catalytic potential to transfer a second mannose molecule
FEBS J.
273
5074-5085
2006
Saccharomyces cerevisiae
brenda
Uccelletti, D.; Farina, F.; Rufini, S.; Magnelli, P.; Abeijon, C.; Palleschi, C.
The Kluyveromyces lactis alpha1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretory pathway
FEMS Yeast Res.
6
449-457
2006
Kluyveromyces lactis
brenda
Kim, M.W.; Kim, E.J.; Kim, J.Y.; Park, J.S.; Oh, D.B.; Shimma, Y.; Chiba, Y.; Jigami, Y.; Rhee, S.K.; Kang, H.A.
Functional characterization of the Hansenula polymorpha HOC1, OCH1, and OCR1 genes as members of the yeast OCH1 mannosyltransferase family involved in protein glycosylation
J. Biol. Chem.
281
6261-6272
2006
Ogataea angusta (Q56VL2), Ogataea angusta
brenda
Song, Y.; Choi, M.H.; Park, J.N.; Kim, M.W.; Kim, E.J.; Kang, H.A.; Kim, J.Y.
Engineering of the yeast Yarrowia lipolytica for the production of glycoproteins lacking the outer-chain mannose residues of N-glycans
Appl. Environ. Microbiol.
73
4446-4454
2007
Yarrowia lipolytica
brenda
Goto, K.; Okawa, Y.
Activity and stability of alpha- and beta-mannosyltransferases in Candida albicans cells cultured at high temperature and at low pH
Biol. Pharm. Bull.
31
1333-1336
2008
Candida albicans, Candida albicans J-1012
brenda
Okamoto, M.; Yoko-o, T.; Miyakawa, T.; Jigami, Y.
The cytoplasmic region of alpha-1,6-mannosyltransferase Mnn9p is crucial for retrograde transport from the Golgi apparatus to the endoplasmic reticulum in Saccharomyces cerevisiae
Eukaryot. Cell
7
310-318
2008
Saccharomyces cerevisiae
brenda
Barnay-Verdier, S.; Beckerich, J.M.; Boisrame, A.
New components of Yarrowia lipolytica Golgi multi-protein complexes containing the alpha-1,6-mannosyltransferases YlMnn9p and YlAnl1p
Curr. Genet.
54
313-323
2008
Yarrowia lipolytica (Q6C286), Yarrowia lipolytica
brenda
Izquierdo, L.; Mehlert, A.; Ferguson, M.A.
The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases
Glycobiology
22
696-703
2012
Trypanosoma brucei
brenda
Striebeck, A.; Robinson, D.A.; Schuettelkopf, A.W.; van Aalten, D.M.
Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis
Open Biology
3
130022
2013
Saccharomyces cerevisiae (P39107), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P39107)
brenda
Zhang, J.; Zhang, Y.; Yang, J.; Kang, L.; EloRM, A.M.; Zhou, H.; Zhao, J.
The alpha-1,6-mannosyltransferase VdOCH1 plays a major role in microsclerotium formation and virulence in the soil-borne pathogen Verticillium dahliae
Fungal Biol.
123
539-546
2019
Verticillium dahliae
brenda
Du, T.; Ouyang, H.; Voglmeir, J.; Wilson, I.B.H.; Jin, C.
Aspergillus fumigatus Mnn9 is responsible for mannan synthesis and required for covalent linkage of mannoprotein to the cell wall
Fungal Genet. Biol.
128
20-28
2019
Aspergillus fumigatus (Q4WIL2), Aspergillus fumigatus, Aspergillus fumigatus ATCC MYA-4609 (Q4WIL2)
brenda