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Information on EC 2.4.1.265 - dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9BVK2

for references in articles please use BRENDA:EC2.4.1.265
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EC Tree
IUBMB Comments
The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
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Homo sapiens
UNIPROT: Q9BVK2
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
halg8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dolichyl-P-Glc:Glc1 Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase
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dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase
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dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase
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ALG8
-
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Dol-P-Glc:Glc1-Man9-GlcNAc2-P-P-Dol glucosyltransferase
-
-
SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-glucosyl phosphate: D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase
The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
malfunction
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ALG8 deficiency (CDG Ih), leads to protein N-glycosylation defects caused by malfunction of Dol-P-Glc:Glc1-Man9-GlcNAc2-P-P-Dol glucosyltransferase resulting in inefficient addition of the second glucose residue onto lipid-linked oligosaccharides. The lipid-linked oligosaccharide profile of the patient shows the accumulation of incomplete precursor structures corresponding to GlcNAc2Man9 and GlcNAc2-Man9Glc1. 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG8_HUMAN
526
10
60088
Swiss-Prot
Secretory Pathway (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
G275D
low residual activity, hypoglycosylation pattern
T47P
low residual activity, hypoglycosylation pattern
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chantret, I.; Dancourt, J.; Dupre, T.; Delenda, C.; Bucher, S.; Vuillaumier-Barrot, S.; Ogier de Baulny, H.; Peletan, C.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E.
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation
J. Biol. Chem.
278
9962-9971
2003
Homo sapiens (Q9BVK2)
Manually annotated by BRENDA team
Vesela, K.; Honzik, T.; Hansikova, H.; Haeuptle, M.A.; Semberova, J.; Stranak, Z.; Hennet, T.; Zeman, J.
A new case of ALG8 deficiency (CDG Ih)
J. Inherit. Metab. Dis.
32
259264
2009
Homo sapiens
Manually annotated by BRENDA team
Schollen, E.; Frank, C.G.; Keldermans, L.; Reyntjens, R.; Grubenmann, C.E.; Clayton, P.T.; Winchester, B.G.; Smeitink, J.; Wevers, R.A.; Aebi, M.; Hennet, T.; Matthijs, G.
Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency)
J. Med. Genet.
41
550-556
2004
Homo sapiens (Q9BVK2)
Manually annotated by BRENDA team
Stlting, T.; Omran, H.; Erlekotte, A.; Denecke, J.; Reunert, J.; Marquardt, T.
Novel ALG8 mutations expand the clinical spectrum of congenital disorder of glycosylation type Ih
Mol. Genet. Metab.
98
305-309
2009
Homo sapiens (Q9BVK2), Homo sapiens
Manually annotated by BRENDA team