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Gene Review

ALG2  -  ALG2, alpha-1,3/1,6-mannosyltransferase

Homo sapiens

Synonyms: Alpha-1,3/1,6-mannosyltransferase ALG2, Asparagine-linked glycosylation protein 2 homolog, CDGIi, FLJ14511, GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase, ...
 
 

ALG2 encodes an alpha1,3 mannosyltransferase involved in the earliest steps of N-glycosylation, the synthesis of the Dolichyl-linked N-glycan precursor.

In the literature, it is frequently confused with ALG-2, Apoptosis Linked Gene 2 (also known as PDCD6) .

 

Disease relevance of ALG2

ALG2 is involved in Congenital Disorder of Glycosylation Ii (  )

 

  • A cell-membrane fraction isolated from Escherichia coli overexpressing thioredoxin-tagged Alg2 was used to demonstrate that this enzyme actually carries out an alpha1,3-mannosylation, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the pathway [1].
 

High impact information on ALG2

  • Expression of wild type but not of mutant hALG2 cDNA restored the mannosyltransferase activity and the biosynthesis of dolichol-linked oligosaccharides both in patient fibroblasts and in the alg2-1 yeast cells. hALG2 was shown to act as an alpha1,3-mannosyltransferase [2].
  • Deficiency of GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (hALG2), is the cause of a new type of congenital disorders of glycosylation (CDG) designated CDG-Ii [2].
 

Biological context of ALG2

(all the entries were related to ALG-2, aka PDCD6)

 

Anatomical context of ALG2

(all the entries were related to ALG-2, aka PDCD6)

 

Associations of ALG2 with chemical compounds

 

Analytical, diagnostic and therapeutic context of ALG2

(all the entries were related to ALG-2, aka PDCD6)

References

  1. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. O'Reilly, M.K., Zhang, G., Imperiali, B. Biochemistry (2006) [Pubmed]
  2. A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis. Thiel, C., Schwarz, M., Peng, J., Grzmil, M., Hasilik, M., Braulke, T., Kohlschütter, A., von Figura, K., Lehle, L., Körner, C. J. Biol. Chem. (2003) [Pubmed]
 
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