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Literature summary for 2.4.1.258 extracted from

  • Ohashi, T.; Nakakita, S.; Sumiyoshi, W.; Takegawa, K.
    Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe (2010), J. Biotechnol., 150, 348-356.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe Q9Y7I4
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-

Synonyms

Synonyms Comment Organism
Alg3
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Schizosaccharomyces pombe

General Information

General Information Comment Organism
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 Schizosaccharomyces pombe