2.4.1.142: chitobiosyldiphosphodolichol beta-mannosyltransferase
This is an abbreviated version!
For detailed information about chitobiosyldiphosphodolichol beta-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.142
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2.4.1.142
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oligosaccharide
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n-glycosylation
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mannosylation
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dolichol-linked
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lipid-linked
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n-linked
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n-glycans
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asparagine-linked
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disease-causing
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glycosylphosphatidylinositol
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glycolipids
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rough
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pharmacology
- 2.4.1.142
- oligosaccharide
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n-glycosylation
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mannosylation
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dolichol-linked
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lipid-linked
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n-linked
- n-glycans
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asparagine-linked
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disease-causing
- glycosylphosphatidylinositol
- glycolipids
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rough
- pharmacology
Reaction
Synonyms
ALG1, ALG1 beta1,4 mannosyltransferase, Alg1 mannosyltransferase, Alg1 protein, Alg1p, beta-1,4 mannosyltransferase, beta1,4-MT, chitobiosyldiphosphodolichol beta-mannosyltransferase, GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-dolichol diphosphochitobiose mannosyltransferase, guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase-1, guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase, mannosyltransferase I, MT-1, MT-I
ECTree
2.4.1.142 chitobiosyldiphosphodolichol beta-mannosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.142 - chitobiosyldiphosphodolichol beta-mannosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C396Y
the mutation is associated with congenital disorders of glycosylation
D429E
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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
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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
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S1A
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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
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S1A/P20L
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site-directed mutagenesis, no difference in N-glycosylation pattern after the replacement of proline residue is observed compared to the S2A mutant
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V106I/M109L/V110I/V113I/V117I/I120L
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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
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additional information
S150R
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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
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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
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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
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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
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additional information
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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
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