2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase

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For detailed information about dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase, go to the full flat file.

Reaction

Synonyms

ALG6, hALG6

ECTree

     2 Transferases

         2.4 Glycosyltransferases

             2.4.1 Hexosyltransferases

                2.4.1.267 dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase

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Results	in table
152	AA Sequence
2	Application
1	Cloned(Commentary)
1	Crystallization (Commentary)
5	Disease/ Diagnostics
5	General Information
1	General Stability
1	Inhibitors
1	Metals/Ions
11	Organism
5	Pathway
2	PDB ID
14	Protein Variants
1	Reaction
11	Reference
2	Source Tissue
2	Substrates and Products (Substrate)
8	Synonyms
1	Systematic Name

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Application on EC 2.4.1.267 - dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

Homo sapiens

Q9Y672

single nucleotide polymorphisms ALG6 rs10889417 G>A and GALNTL4 rs12270446 G>C independently predict cutaneous melanoma disease-specific survival. The low death-risk-associated rs10889417 A allele is associated with increase in ALG6 mRNA expression levels in cultured skin fibroblasts and whole blood cells and the rs12270446 G allele is associated with decrease in GALNTL4 mRNA expression levels in skin tissues

758995

synthesis

Yarrowia lipolytica

-

genetic engineering of N-glycan biosynthesis in Yarrowia lipolytica so that it produces Man(3)GlcNAc(2) structures on its glycoproteins. Disruption of the ALG3 gene, EC 2.4.1.258, results in modification of proteins mainly with Man(5)GlcNAc(2) and GlcMan(5)GlcNAc(2) glycans, and to a lesser extent with Glc(2)Man(5)GlcNAc(2) glycans. To avoid underoccupancy of glycosylation sites, Alg6, EC 2.4.1.267, is concomitantly overexpressed. Overexpression of the heterodimeric Aspergillus niger glucosidase II results in removal the terminal glucose residues. Overexpression of an alpha-1,2-mannosidase leads to Man(3)GlcNAc(2) structures, which are substrates for the synthesis of complex-type glycans. The final Yarrowia lipolytica strain produces proteins glycosylated with the trimannosyl core N-glycan (Man(3)GlcNAc(2)), which is the common core of all complex-type N-glycans

723575