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Information on EC 2.4.1.258 - dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and Organism(s) Schizosaccharomyces pombe and UniProt Accession Q9Y7I4

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IUBMB Comments
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
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Schizosaccharomyces pombe
UNIPROT: Q9Y7I4
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alg3p, atalg3, tbalg3, dol-p-man:man5glcnac2-pp-dol mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-mannosyl phosphate: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 alpha-1,3-mannosyltransferase
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
deletion of the alg3+ gene in the och1 deletion mutant lacking alpha-1,6mannosyltransferase activity. Analysis of the detailed oligosaccharide structures in alg3och1 double mutant reveals that the N-linked oligosaccharides of Schizosaccharomyces pombe alg3och1 cells mainly consist of two or three alpha-galactose-capped M5B structures. Western blot analysis of recombinant human transferrin in alg3och1 cells suggests that heterologously expressed glycoproteins in this mutant have Endo H-resistant N-linked oligosaccharide structures similar to those of alg3och1 cell-surface glycoproteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ohashi, T.; Nakakita, S.; Sumiyoshi, W.; Takegawa, K.
Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe
J. Biotechnol.
150
348-356
2010
Schizosaccharomyces pombe (Q9Y7I4)
Manually annotated by BRENDA team