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.
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
2.4.1.267 dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.267 - dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A333V
analysis of lipid-linked oligosaccharides in cultured fibroblasts indicates accumulation of Man9GlcNAc2-PP-Dol. Sequence analysis of ALG6 reveals a deletion of exon 3 (c.257 + 5G > A) in combination with a missense mutation (c.998C > T, p.Ala333Val). The patient shows skeletal dysplasia with brachytelephalangy
delI299/F304S
patient with three mutations in the hALG6 gene. The maternal allele has an intronic G -> A mutation resulting in skipping of exon3 (IVS3 + 5G > A). This produces a nonfunctional enzyme as shown by its inability to restore normal glycosylation in a Saccharomyces cerevisiae strain lacking a functional ALG6. The paternal allele has two mutations. One is a deletion of three bases (895897delATA) leading to an in-frame deletion of isoleucine 299 (delI299) located in a transmembrane domain. The second mutation on the same allele 911T > C causes a F304S change. When expressed in the ALG6 deficient yeast strain, this allele restores glycosylation but the mRNA is unstable or inefficiently transcribed, contributing to the impaired glycosylation in the patient
F304S
natural variant, common polymorphism reduces the ability to rescue defective glycosylation of an alg6-deficient strain of S. cerevisiae during rapid growth, may exacerbate the clinical severity of patients with CDG1A
Y131H
frequent natural variant, the cause of congenital disorder of glycosylation-Ic (CDG-Ic). One patient with typical CDG-Ic symptoms and a homozygous p.Tyr131His alteration in ALG6. In contrast to most CDG patients, her LLO and plasma transferrin glycosylation appeared normal. Thus, it is unclear whether Y131H causes CDG-Ic or contributes to the symptoms
