2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
This is an abbreviated version!
For detailed information about dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.267
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2.4.1.267
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cdg-ic
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oligosaccharide
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lipid-linked
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n-glycosylation
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croatian
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n-linked
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synthesis
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medicine
- 2.4.1.267
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cdg-ic
- oligosaccharide
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lipid-linked
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n-glycosylation
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croatian
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n-linked
- synthesis
- medicine
Reaction
Synonyms
ALG6, hALG6
ECTree
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General Information
General Information on EC 2.4.1.267 - dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
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malfunction
physiological function
malfunction
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alg6-1 mutants accumulate Man9GlcNAc2-P-P-dolichol as their largest lipid-linked oligosaccharide in vivo and in vitro. alg6-1 cells are unable to transfer glucose from dolichol phosphoglucose to the unglucosylated lipid-linked oligosaccharide
ALG6 deficient MI8-5 cells express 2fold lower levels of oligosaccharyltransferase STT3B than the parental Chinese hamster ovary cells. The combination of reduced expression of STT3B and the lack of the optimal Dol-PP-GlcNAc2Man9Glc3 donor synergize to cause very severe hypoglycosylation of proteins in MI8-5 cells
physiological function
fibroblasts from an ALG6-congenital disorders of glycosylation patient that carries the A333V mutation on the maternal ALG6 allele and the S308R and Y131H mutations on the paternal ALG6 allele assemble Dol-PP-GlcNAc2Man9 as the largest oligosaccharide donor. 3040% of oligosaccharyltransferase STT3A-dependent glycosylation sites and 20% of oligosaccharyltransferase STT3B-dependent sites are skipped in ALG6-congenital disorders of glycosylation fibroblasts
physiological function
three-state mechanism, where Dol-P-Glc binds before the Man9-containing acceptor substrate, because the glucose moiety is at the bottom of the active site cavity. Donor and acceptor substrates bind sequentially and Asp69 acts as a general base that abstracts the proton of the 3-hydroxyl group of the terminal A-branch mannose of the acceptor substrate to activate it for a nucleophilic attack