Any feedback?
No. of entries
Information on EC 2.4.1.142 - chitobiosyldiphosphodolichol beta-mannosyltransferase
for references in articles please use BRENDA:EC2.4.1.142
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.142 chitobiosyldiphosphodolichol beta-mannosyltransferase
The enzyme appears in viruses and cellular organisms
- 2.4.1.142
- oligosaccharide
-
n-glycosylation
-
mannosylation
-
dolichol-linked
-
lipid-linked
-
n-linked
- n-glycans
-
asparagine-linked
-
disease-causing
- glycosylphosphatidylinositol
- glycolipids
-
rough
- pharmacology
Reaction Schemes
showSynonyms
alg1 protein, mannosyltransferase i, chitobiosyldiphosphodolichol beta-mannosyltransferase, alg1 beta1,4 mannosyltransferase, alg1p, gdp-man:glcnac2-pp-dolichol mannosyltransferase, alg1 mannosyltransferase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALG1
Alg1p
beta-1,4 mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
-
-
-
-
guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase-1
-
guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol = GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
protein N-glycosylation initial phase (eukaryotic)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:chitobiosyldiphosphodolichol beta-D-mannosyltransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
83380-85-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
GDP-alpha-D-mannose + diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
GDP + beta-(1->4)-D-mannosylchitobiosyl diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the molecular nature of severe multisystemic disorder with a recurrent nonimmune hydrops fetalis is identified as deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase caused by a C773T transition
Products: -
Products: -
?
additional information
?
-
-
Substrates: patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be referred to as CDG-Ik
Products: -
Products: -
?
additional information
?
-
-
Substrates: two distinct complexes that contain multiple copies of Alg1 mannosyltransferase are identified. The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11. Physical association of the functionally related catalytic enzymes involved in lipid-linked oligosaccharide synthesis provides an additional level of regulation that assures proper construction of the complex oligosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Comparison to the reaction of dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A (EC 2.4.99.18)
Products: -
Products: -
?
additional information
?
-
Substrates: Alg1 protein transfers a second beta-linkage mannose to the GlcNAc2-PP-Phy (phytanyl-diphosphoryl-alpha-N, N'-diacetylchitobioside) substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Alg1 protein transfers a second beta-linkage mannose to the GlcNAc2-PP-Phy (phytanyl-diphosphoryl-alpha-N, N'-diacetylchitobioside) substrate
Products: -
Products: -
?
additional information
?
-
Substrates: chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Comparison to the reaction of dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit STT3A (EC 2.4.99.18)
Products: -
Products: -
?
additional information
?
-
Substrates: Alg1 protein transfers a second beta-linkage mannose to the GlcNAc2-PP-Phy (phytanyl-diphosphoryl-alpha-N, N'-diacetylchitobioside) substrate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
GDP + beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphosphodolichol
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the molecular nature of severe multisystemic disorder with a recurrent nonimmune hydrops fetalis is identified as deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase caused by a C773T transition
Products: -
Products: -
?
additional information
?
-
-
Substrates: patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be referred to as CDG-Ik
Products: -
Products: -
?
additional information
?
-
-
Substrates: two distinct complexes that contain multiple copies of Alg1 mannosyltransferase are identified. The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11. Physical association of the functionally related catalytic enzymes involved in lipid-linked oligosaccharide synthesis provides an additional level of regulation that assures proper construction of the complex oligosaccharides
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik.
Pemphigoid, Bullous
A successful treatment with ustekunumab in a case of anti-laminin-?1 pemphigoid associated with psoriasis.
Psoriasis
A successful treatment with ustekunumab in a case of anti-laminin-?1 pemphigoid associated with psoriasis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
tissue specific enzyme expression analysis: the HMT-1 expression is generally upregulated in liver, kidney, spleen, pancreas, testis and ovary, possibly reflecting high demand of N-glycans for proteins produced in these tissues. Inversely, its expression is downregulated in skeletal muscle, thymus, prostate and small intestine for unknown reason
brenda
additional information
-
tissue specific enzyme expression analysis: the HMT-1 expression is generally upregulated in liver, kidney, spleen, pancreas, testis and ovary, possibly reflecting high demand of N-glycans for proteins produced in these tissues. Inversely, its expression is downregulated in skeletal muscle, thymus, prostate and small intestine for unknown reason
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
ER, the predicted transmembrane domain localizes the N-terminus of Alg1 into the ER lumen. The N-terminal transmembrane domain including the following positively charged amino acids and an N-terminal amphiphilic-like alpha-helix domain exposed on the protein surface strictly coordinate the Alg1 orientation on the ER membrane. The N- and C-termini of Alg1 are located to luminal and cytosolic side of the ER, respectively. The conserved proline 20 residue has no effect on its membrane-spanning property. The positively charged amino acids (K35, K38, K39 and R40) downstream of the N-terminal transmembrane region are important for ER membrane attachment
brenda
-
ER, the predicted transmembrane domain localizes the N-terminus of Alg1 into the ER lumen. The N-terminal transmembrane domain including the following positively charged amino acids and an N-terminal amphiphilic-like alpha-helix domain exposed on the protein surface strictly coordinate the Alg1 orientation on the ER membrane. The N- and C-termini of Alg1 are located to luminal and cytosolic side of the ER, respectively. The conserved proline 20 residue has no effect on its membrane-spanning property. The positively charged amino acids (K35, K38, K39 and R40) downstream of the N-terminal transmembrane region are important for ER membrane attachment
-
brenda
membrane topology of Alg1, overview. A conserved alpha-helix domain, Alg1 Nalpha3 domain, contributes to the membrane association of Alg1 protein
brenda
-
membrane topology of Alg1, overview. A conserved alpha-helix domain, Alg1 Nalpha3 domain, contributes to the membrane association of Alg1 protein
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
for proper accomplishment of protein N-glycosylation, early assembly of dolichol-linked oligosaccharides on cytoplasmic side of the rough endoplasmic reticulum membrane must progress at a rate greater than subsequent flipping of dolichol-linked oligosaccharides into luminal side. To assure this, all activities of five glycosyltransferases involved in early DLO assembly are required in addition to their substrates. If any of them is diminished, eukaryotic cell would not be able to survive
physiological function
additional information
malfunction
a deficiency in guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase-1 causes type I congenital disorders of glycosylation
malfunction
ALG1-congenital disorders is a subtype with severe multiorgan involvement (OMIM 608540) caused by pathogenic variants in ALG1. It is caused by non-functional alternative splicing involving a pathogenic complex allele
physiological function
the enzyme is involved in the early assembly of dolichol-linked oligosaccharides. Early dolichol-linked oligosaccharide assembly from dolichyl phosphate to Man5GlcNAc2-PP-Dol is a fundamental and essential event for viability of eukaryotic cells, especially multicellular organisms. Analysis of transcriptional regulation, overview. The 200 bp region upstream from HMT-1 open reading frame is crucial for both positive and negative regulation of the HMT-1 transcription
physiological function
ALG1 is presumed to be involved in the regulation of the protein N-glycosylation. Genetic association of WDR3 and ALG1 in schizophrenia. The WDR3 gene may likely be a sensitive factor in female patients with schizophrenia
physiological function
ALG1 is presumed to be involved in the regulation of the protein N-glycosylation. Genetic association of WDR3 and ALG1 in schizophrenia
additional information
Alg1, a beta-1,4 mannosyltransferase (MTase), physically interacts with Alg2 (EC 2.4.1.132) and Alg11 (EC 2.4.1.257) proteins to form the multienzyme complex which catalyzes the addition of all five mannose to generate the Man5GlcNAc2-PP-Dol intermediate. Alg1 plays a central role in the formation of the multi-MTase, the topological information of Alg1 including the molecular mechanism of membrane association is analyzed. Alg1 shares structure similarity with Alg13/14 complex, which has been defined as a membrane-associated GT-B GTase, structural similarities, overview
additional information
-
Alg1, a beta-1,4 mannosyltransferase (MTase), physically interacts with Alg2 (EC 2.4.1.132) and Alg11 (EC 2.4.1.257) proteins to form the multienzyme complex which catalyzes the addition of all five mannose to generate the Man5GlcNAc2-PP-Dol intermediate. Alg1 plays a central role in the formation of the multi-MTase, the topological information of Alg1 including the molecular mechanism of membrane association is analyzed. Alg1 shares structure similarity with Alg13/14 complex, which has been defined as a membrane-associated GT-B GTase, structural similarities, overview
additional information
-
Alg1, a beta-1,4 mannosyltransferase (MTase), physically interacts with Alg2 (EC 2.4.1.132) and Alg11 (EC 2.4.1.257) proteins to form the multienzyme complex which catalyzes the addition of all five mannose to generate the Man5GlcNAc2-PP-Dol intermediate. Alg1 plays a central role in the formation of the multi-MTase, the topological information of Alg1 including the molecular mechanism of membrane association is analyzed. Alg1 shares structure similarity with Alg13/14 complex, which has been defined as a membrane-associated GT-B GTase, structural similarities, overview
-
Show AA Sequence and Transmembrane Helices (2629 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
two distinct complexes that contain multiple copies of Alg1 mannosyltransferase are identified. The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11. Alg1 self-assembles through a C-terminal domain that is distinct from the region required for its association with Alg2 or Alg11
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C396Y
the mutation is associated with congenital disorders of glycosylation
D429E
-
patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be reffered to as CDG-Ik
E342L
mutation in the semiconserved regions of the HMT-1 gene causes drastically reduced enzyme activity, leading to a severe disease with death in early infancy
G145D
the mutation is associated with congenital disorders of glycosylation
M377V
the mutation is associated with congenital disorders of glycosylation
R276W
the mutation is associated with congenital disorders of glycosylation
R438W
the mutation is associated with congenital disorders of glycosylation
S150R
S258L
K35A/K38A/K39A/R40A/V106I/M109L/V110I/V113I/V117I/I120L
site-directed mutagenesis, hydrophobic mut6 substitution of truncation mutant Alg1DELTA32 with additional mutations K35A, K38A, K39A, R40A. The mutant shows slower growth and decreased protein amount in membrane fraction compared to mutant Alg1NDELTA32-mut6A
S1A
site-directed mutagenesis, the N-terminal S2A-inserted Alg1p (FLAG-S2A-Alg1) is N-glycosylated by confirming the shift of protein band after PNGase treatment, whereas the C-terminal inserted form (Alg1-S2A-FLAG) is not
S1A/P20L
site-directed mutagenesis, no difference in N-glycosylation pattern after the replacement of proline residue is observed compared to the S2A mutant
V106I/M109L/V110I/V113I/V117I/I120L
site-directed mutagenesis, hydrophobic mut6 substitution of truncation mutant Alg1DELTA40, Alg1NDELTA40-mut6A is barely detected in either the membrane fraction or the cytosolic fraction, indicating that this mutant protein has been degraded. Alg1NDELTA40-mut6A mutant protein shows activity in vitro. Alg1NDELTA32-mut6A appears to function similar to intact Alg1 at 30°C and a similar expression level as wild-type Alg1
K35A/K38A/K39A/R40A/V106I/M109L/V110I/V113I/V117I/I120L
-
site-directed mutagenesis, hydrophobic mut6 substitution of truncation mutant Alg1DELTA32 with additional mutations K35A, K38A, K39A, R40A. The mutant shows slower growth and decreased protein amount in membrane fraction compared to mutant Alg1NDELTA32-mut6A
-
S1A
-
site-directed mutagenesis, the N-terminal S2A-inserted Alg1p (FLAG-S2A-Alg1) is N-glycosylated by confirming the shift of protein band after PNGase treatment, whereas the C-terminal inserted form (Alg1-S2A-FLAG) is not
-
S1A/P20L
-
site-directed mutagenesis, no difference in N-glycosylation pattern after the replacement of proline residue is observed compared to the S2A mutant
-
V106I/M109L/V110I/V113I/V117I/I120L
-
site-directed mutagenesis, hydrophobic mut6 substitution of truncation mutant Alg1DELTA40, Alg1NDELTA40-mut6A is barely detected in either the membrane fraction or the cytosolic fraction, indicating that this mutant protein has been degraded. Alg1NDELTA40-mut6A mutant protein shows activity in vitro. Alg1NDELTA32-mut6A appears to function similar to intact Alg1 at 30°C and a similar expression level as wild-type Alg1
-
additional information
S150R
-
patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be reffered to as CDG-Ik
S150R
the mutation is associated with congenital disorders of glycosylation
S258L
mutation in the semiconserved regions of the HMT-1 gene causes drastically reduced enzyme activity, leading to a severe disease with death in early infancy
S258L
-
patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be reffered to as CDG-Ik
S258L
the mutation is associated with congenital disorders of glycosylation
additional information
-
the molecular nature of severe multisystemic disorder with a recurrent nonimmune hydrops fetalis is identified as deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase caused by the C773T transition
additional information
genotyping 10 single nucleotide polymorphisms from gene ALG1 are identified using the Japanese case-control sample (1808 schizophrenics and 2170 matched controls). Genotype-phenotype correlation analysis in schizophrenia patients, overview
additional information
-
genotyping 10 single nucleotide polymorphisms from gene ALG1 are identified using the Japanese case-control sample (1808 schizophrenics and 2170 matched controls). Genotype-phenotype correlation analysis in schizophrenia patients, overview
additional information
chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 (from human, EC 2.4.1.257), and Alg11 (from yeast, EC 2.4.1.131) proteins, chemo-enzymatic synthesis strategy to extend the glycan moiety of synthetic LLO analogues to Dol-PP-GlcNAc2Man5, method, overview
additional information
deletion of the first 32 (alg1NDELTA32), 40 (alg1NDELTA40) or 50 (alg1NDELTA50) amino acids of Alg1p. Alg1NDELTA32 protein lacks the predicted N-terminal transmembrane domain, and further deletion of additional eight amino acids, including four positively charged residues, results in Alg1NDELTA40. Moreover, in Alg1NDELTA50, the first beta-sheet of Alg1 is completely eliminated. Mutant alg1NDELTA50 fails to rescue cell growth at the 30°C. Cells expressing alg1NDELTA32 show normal growth, similar to those expressing full-length Alg1, at normal temperature of 30°C and also relatively similar protein expression level. However, when the temperature is raised to 37°C, alg1NDELTA32-expressing cells show an obvious growth defect. The alg1NDELTA40-expressing cells exhibit a similar growth state as wild-type Alg1-expressing cells at 30°C, but partially affected growth at 37°C. Alg1NDELTA40 associates with the endoplasmic reticulum membrane in a nonperipheral manner, as does wild-type Alg1
additional information
-
deletion of the first 32 (alg1NDELTA32), 40 (alg1NDELTA40) or 50 (alg1NDELTA50) amino acids of Alg1p. Alg1NDELTA32 protein lacks the predicted N-terminal transmembrane domain, and further deletion of additional eight amino acids, including four positively charged residues, results in Alg1NDELTA40. Moreover, in Alg1NDELTA50, the first beta-sheet of Alg1 is completely eliminated. Mutant alg1NDELTA50 fails to rescue cell growth at the 30°C. Cells expressing alg1NDELTA32 show normal growth, similar to those expressing full-length Alg1, at normal temperature of 30°C and also relatively similar protein expression level. However, when the temperature is raised to 37°C, alg1NDELTA32-expressing cells show an obvious growth defect. The alg1NDELTA40-expressing cells exhibit a similar growth state as wild-type Alg1-expressing cells at 30°C, but partially affected growth at 37°C. Alg1NDELTA40 associates with the endoplasmic reticulum membrane in a nonperipheral manner, as does wild-type Alg1
additional information
-
chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 (from human, EC 2.4.1.257), and Alg11 (from yeast, EC 2.4.1.131) proteins, chemo-enzymatic synthesis strategy to extend the glycan moiety of synthetic LLO analogues to Dol-PP-GlcNAc2Man5, method, overview
-
additional information
-
deletion of the first 32 (alg1NDELTA32), 40 (alg1NDELTA40) or 50 (alg1NDELTA50) amino acids of Alg1p. Alg1NDELTA32 protein lacks the predicted N-terminal transmembrane domain, and further deletion of additional eight amino acids, including four positively charged residues, results in Alg1NDELTA40. Moreover, in Alg1NDELTA50, the first beta-sheet of Alg1 is completely eliminated. Mutant alg1NDELTA50 fails to rescue cell growth at the 30°C. Cells expressing alg1NDELTA32 show normal growth, similar to those expressing full-length Alg1, at normal temperature of 30°C and also relatively similar protein expression level. However, when the temperature is raised to 37°C, alg1NDELTA32-expressing cells show an obvious growth defect. The alg1NDELTA40-expressing cells exhibit a similar growth state as wild-type Alg1-expressing cells at 30°C, but partially affected growth at 37°C. Alg1NDELTA40 associates with the endoplasmic reticulum membrane in a nonperipheral manner, as does wild-type Alg1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His10-tagged enzyme ALG1 from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant hALG1 in Saccharomyces cerevisiae alg1-1 strain
-
gene ALG1, located on chromosome 16p13.3, genomic structure, genotyping. Gene-gene interaction analysis of genes ALG1 and WDR3
gene Alg1, recombinant expression of GFP-tagged enzyme in Saccharomyces cerevisiae, recombinant expression of His6- or FLAG-tagged Alg1 mutants in Saccharomyces cerevisiae strain XGY29, in which chromosomal ALG1 is under the control of the glucose-repressible GAL1/10 promoter
gene ALG1, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21-Gold (DE3)
gene HMT-1, DNA and amino acid sequence determination and analysis, cloning from HeLa cells, subcloning in Escherichia coli strain JM109. Detection of potential cis-acting motifs in a 1 kb region upstream from initiation codon of the HMT-1 and analysis of transcriptional regulation of gene HMT-1, determination of initiation site for the HMT-1 transcription, overview. Semi-quantitative RT-PCR enzyme expression analysis. Expression profile of the HMT-1 among various tissues, overview
glycosylation and growth of Alg1-deficient PRY56 yeast cells, showing a temperature-sensitive phenotype, can be restored by the human wild-type allele, only slight restoration is observed after transformation with the patients allelles. One patient has homozygous point mutation S258L, the other patient is compound heterozygous for the mutations S258L and E342O. Mutation in the semiconserved regions of the HMT-1 gene causes drastically reduced enzyme activity, leading to a severe disease with death in early infancy
patient with congenital disorder of glycosylation is compound heterozygous for three mutations in the ALG1 gene, leading to the amino acid substitutions S150R and D429E on one allele and S258L on the other. The detrimental effect of these mutations on ALG1 protein function is demonstrated in a complementation assay. This novel type of congenital disorder of glycosylation should be reffered to as CDG-Ik
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chitobiosyldiphosphodolichol beta-mannosyltransferase (ALG1) mRNAs are upregulated greater in the adult (postnatal days 50) than in the infant (postnatal days 8) rats by schizophrenomimetics, methamphetamine and phencyclidine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
the WD repeat domain 3 (WDR3) and chitobiosyldiphosphodolichol beta-mannosyltransferase (ALG1) genes are target candidates for schizophrenia-related molecules, whose mRNAs are upregulated in the adult (postnatal week seven), but not in the infant (postnatal week one) rats by an indirect dopamine agonist, and phencyclidine, an antagonist of the NMDA receptor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaushal, G.P.; Elbein, A.D.
Purification and properties of beta-mannosyltransferase that synthesizes Man-beta-GlcNAc-GlcNAc-pyrophosphoryl-dolichol
Arch. Biochem. Biophys.
250
38-47
1986
Sus scrofa
brenda
Kaushal, G.P.; Elbein, A.D.
Partial purification and characterization of beta-mannosyltransferase from suspension-cultured soybean cells
Biochemistry
26
7953-7960
1987
Glycine max
brenda
Schwarz, M.; Thiel, C.; Lubbehusen, J.; Dorland, B.; de Koning, T.; von Figura, K.; Lehle, L.; Korner, C.
Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik
Am. J. Hum. Genet.
74
472-481
2004
Homo sapiens
brenda
Kranz, C.; Denecke, J.; Lehle, L.; Sohlbach, K.; Jeske, S.; Meinhardt, F.; Rossi, R.; Gudowius, S.; Marquardt, T.
Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I
Am. J. Hum. Genet.
74
545-551
2004
Homo sapiens (Q9BT22), Homo sapiens
brenda
Takahashi, T.; Honda, R.; Nishikawa, Y.
Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1
Glycobiology
10
321-327
2000
Homo sapiens (Q9BT22), Homo sapiens
brenda
Gao, X.D.; Nishikawa, A.; Dean, N.
Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum
Glycobiology
14
559-570
2004
Saccharomyces cerevisiae
brenda
Grubenmann, C.E.; Frank, C.G.; Huelsmeier, A.J.; Schollen, E.; Matthijs, G.; Mayatepek, E.; Berger, E.G.; Aebi, M.; Hennet, T.
Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik
Hum. Mol. Genet.
13
535-542
2004
Homo sapiens
brenda
Dupre, T.; Vuillaumier-Barrot, S.; Chantret, I.; Yaye, H.S.; Le Bizec, C.; Afenjar, A.; Altuzarra, C.; Barnerias, C.; Burglen, L.; de Lonlay, P.; Feillet, F.; Napuri, S.; Seta, N.; Moore, S.E.
Guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase deficiency (congenital disorders of glycosylation type Ik): five new patients and seven novel mutations
J. Med. Genet.
47
729-735
2010
Homo sapiens (Q9BT22)
brenda
Takahashi, T.; Nedachi, T.; Etoh, T.; Tachikawa, H.; Gao, X.D.
Identification and characterization of transcriptional control region of the human beta 1,4-mannosyltransferase gene
Cytotechnology
69
417-434
2017
Homo sapiens (Q9BT22), Homo sapiens
brenda
Ramirez, A.S.; Boilevin, J.; Lin, C.W.; Ha Gan, B.; Janser, D.; Aebi, M.; Darbre, T.; Reymond, J.L.; Locher, K.P.
Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins
Glycobiology
27
726-733
2017
Saccharomyces cerevisiae (P16661), Saccharomyces cerevisiae ATCC 204508 (P16661)
brenda
Xu, X.X.; Li, S.T.; Wang, N.; Kitajima, T.; Yoko-O, T.; Fujita, M.; Nakanishi, H.; Gao, X.D.
Structural and functional analysis of Alg1 beta-1,4 mannosyltransferase reveals the physiological importance of its membrane topology
Glycobiology
28
741-753
2018
Saccharomyces cerevisiae (P16661), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P16661)
brenda
Kobayashi, M.; Jitoku, D.; Iwayama, Y.; Yamamoto, N.; Toyota, T.; Suzuki, K.; Kikuchi, M.; Hashimoto, T.; Kanahara, N.; Kurumaji, A.; Yoshikawa, T.; Nishikawa, T.
Association studies of WD repeat domain 3 and chitobiosyldiphosphodolichol beta-mannosyltransferase genes with schizophrenia in a Japanese population
PLoS ONE
13
e0190991
2018
Homo sapiens (Q9BT22), Homo sapiens, Rattus norvegicus (D4A5S6)
brenda
Gonzalez-Dominguez, C.A.; Fiesco-Roa, M.O.; Gomez-Carmona, S.; Kleinert-Altamirano, A.P.I.; He, M.; Daniel, E.J.P.; Raymond, K.M.; Abreu-Gonzalez, M.; Manrique-Hernandez, S.; Gonzalez-Jaimes, A.; Salinas-Marin, R.; Molina-Garay, C.; Carrillo-Sanchez, K.; Flores-Lagunes, L.L.; Jimenez-Olivares, M.; Munoz-Rivas, A.; Cruz-Munoz, M.E.; Ruiz-Garcia, M.; Freeze, H.H.; Mora-Montes, H.M.; Alaez-Verson, C.; Martnez-Duncker, I.
ALG1-CDG caused by non-functional alternative splicing involving a novel pathogenic complex allele
Front. Genet.
12
744884
2021
Homo sapiens (Q9BT22)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.142)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
