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Information on EC 2.4.1.131 - GDP-Man:Man3GlcNAc2-PP-dolichol alpha-1,2-mannosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q2TAA5

for references in articles please use BRENDA:EC2.4.1.131
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IUBMB Comments
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
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This record set is specific for:
Homo sapiens
UNIPROT: Q2TAA5
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Word Map
  • 2.4.1.131
  • lipid-linked
  • n-glycosylation
  • n-linked
  • glycosyltransferase
  • dolichol-linked
  • asparagine-linked
  • man5glcnac2-pp-dolichol
  • alpha1,2-linked
  • single-subunit
  • oligosaccharyltransferase
  • man5glcnac2-pp-dol
  • microcephaly
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
alg11, halg11, gdp-man:man3glcnac2-pp-dolichol-alpha1,2-mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-Man:Man3GlcNAc2-PP-dolichol-alpha1,2-mannosyltransferase
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GDP-mannose-oligosaccharide-lipid mannosyltransferase
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guanosine diphosphomannose-oligosaccharide-lipid mannosyltransferase
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mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid
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oligosaccharide-lipid mannosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose:D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 2-alpha-D-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
CAS REGISTRY NUMBER
COMMENTARY hide
74506-43-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a patient with muscular hypotonia, convulsions, developmental retardation, dysmorphic signs and death in infancy, a deficiency of GDP-Man:Man3GlcNAc2-PP-dolichol mannosyltransferase, the human ortholog of Alg11 from yeast, is identified as the molecular cause. The enzymatic malfunction leads to impairment in the elongation of lipid-linked oligosaccharides at the outer leaflet of the endoplasmic reticulum, resulting in CDG-Ip, a congenital disorders of glycosylation. Mutation p.L86S in the endoplasmic reticulum mannosyltransferase hALG11 leads to accumulation of Man3GlcNAc2-PP-dolichol and Man4GlcNAc2-PP-dolichol in the index CDG-Ip patient
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG11_HUMAN
492
2
55651
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L85A
no effect on Alg11 mannosyltransferase activity
L86P
mutant enzyme does not complement the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
L86S
mutant enzyme slightly complements the growth deffect of the mutant strain DELTAalgg3 (Saccharomyces cerevisiae)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
retroviral expression of human wild-type and mutated ALG11 cDNA in patient-derived fibroblasts as well as using a yeast alg11 deletion strain as a heterologous expression system for hALG11 variants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rind, N.; Schmeiser, V.; Thiel, C.; Absmanner, B.; Lbbehusen, J.; Hocks, J.; Apeshiotis, N.; Wilichowski, E.; Lehle, L.; Krner, C.
A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip
Hum. Mol. Genet.
19
1413-1424
2010
Homo sapiens (Q2TAA5), Homo sapiens
Manually annotated by BRENDA team