EC Number   |
Protein Variants |
Reference |
|---|
   2.4.1.265 | A282V |
CDG type Ih is caused by a deficiency of the dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase. The defect leads to an accumulation of Dol-PP-Glc-NAc2Man9 and Dol-PP-GlcNAc2Man9Glc1 in the endoplasmic reticulum of patients fibroblasts that can be detected by analyzing the lipid-linked oligosaccharyl intermediates. Two mildly affected siblings with CDG-Ih caused by two novel mutations are described. While one mutation (c.1434delC) causes a frame shift resulting in a premature termination codon (p.485X), the point mutation of the other allele (c.845C>T, p.A282V) causes an amino acid replacement in a highly conserved region of the hALG8 gene. The two siblings show similar symptoms, including pseudo-gynecomastia, epicanthus, muscular hypotonia, mental retardation and ataxia, expanding the genetic and clinical spectrum of CDG-Ih |
709971 |
| 2.4.1.265 | G275D |
low residual activity, hypoglycosylation pattern |
709484 |
| 2.4.1.265 | R364X |
two ALG8 mutations in heterozygous form are detected in the patient. The first mutation (c.139A>C), is combined with a c.1090C>T mutation. The index mutation, which is translated into the missense mutation p.T47P, is inherited from the father. The c.1090C>T mutation resulting in a premature stop codon (p.R364X) is found in heterozygous form in the mother, whereas it is not found in 150 healthy controls. The prognosis of patients with ALG8 deficiency is unfavourable. The majority of affected children have early onset of the disease with heterogeneous symptoms including multiple organ dysfunction, coagulopathy and protein-losing enteropathy |
709391 |
| 2.4.1.265 | T47P |
low residual activity, hypoglycosylation pattern |
709484 |
