Information on EC 2.4.1.131 - GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53954
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The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Comparison to the reaction of dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A (EC 2.4.99.18)
involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-2)Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcalpha/beta is the product of the middle-arm terminal alpha1,2-mannosyltransferase Alg9p
2 GDP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
involved in asparagine-linked glycosylation, reaction proceeds in the endoplasmatic reticulum, role of the ALG9 step in downstream ER and Golgi N-glycan processing events
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side
a deletion of the ALG11 gene leads to poor growth and temperature-sensitive lethality, disruption of the ALG11 locus results in Underglycosylation of proteins
compared with wild-type cells, DELTAalg11 grows poorly and osmotic stabilization by KCl only slightly improved growth. Deletion of ALG11 causes a temperature-sensitive lethality between 32°C and 36°C
the protein is predicted to contain four N-linked glycosylation sites, but none appear to be utilized, because Alg11p is insensitive to digestion with endo H
recombinant N-terminally His10-tagged enzyme ALG11 from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a plasmid pREP1+/-ALG11HA for the expression of Saccharomyces cerevisiae ALG11 in Schizosaccharomyces pombe and introducing it into gmd3 mutant. The gmd3 mutant, carrying pREP+/-ALG11HA, grows at 37°C, whereas the gmd3 mutant, carrying vector pREP1 alone, does not. The defect in acid phosphatase glycosylation of gmd3 mutant is also suppressed by Saccharomyces cerevisiae ALG11. The gmd3+/alg11+ gene is a functional homologue of the Saccharomyces cerevisiae ALG11 gene
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
The Saccharomyces cerevisiae alg12delta mutant reveals a role for the middle-arm alpha1,2Man- and upper-arm alpha1,2Manalpha1,6Man-residues of Glc(3)Man(9)GlcNAc(2)-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus
Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide
Cipollo, J.F.; Trimble, R.B.; Chi, J.H.; Yan, Q.; Dean, N.
The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum
Umeda, K.; Yoko-o, T.; Nakayama, K.; Suzuki, T.; Jigami, Y.
Schizosaccharomyces pombe gmd3(+)/alg11(+) is a functional homologue of Saccharomyces cerevisiae ALG11 which is involved in N-linked oligosaccharide synthesis