Information on EC 2.4.1.142 - chitobiosyldiphosphodolichol beta-mannosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.142
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RECOMMENDED NAME
GeneOntology No.
chitobiosyldiphosphodolichol beta-mannosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein N-glycosylation (eukaryotic, high mannose)
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dolichyl-diphosphooligosaccharide biosynthesis
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N-Glycan biosynthesis
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Various types of N-glycan biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:chitobiosyldiphosphodolichol beta-D-mannosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
83380-85-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a deficiency in guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase-1 causes type I congenital disorders of glycosylation
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
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
show the reaction diagram
GDP-mannose + diphosphodolichyl-N-acetyl-D-glucosaminyl-N-acetyl-D-glucosamine
GDP + beta-(1->4)-D-mannosylchitobiosyl diphosphodolichol
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GDP-mannose + chitobiosyldiphosphodolichol
GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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less stimulatory than Mg2+
Mn2+
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less stimulatory than Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP-glucose
p-chloromercuribenzenesulfonic acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NP-40
phosphatidic acid
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phosphatidylcholine
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phosphatidylserine
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Phospholipid
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Triton X-100
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optimum activity at 0.08-0.1%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 0.0017
GDP-mannose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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fetal
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18ºC, 0.5 mM DTT, 20% glycerol, several weeks
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frozen, Tris-buffer, pH 7.0, 0.5 mM DTT, 20% glycerol, 0.1% detergent, 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose, epoxy-activated-Sepharose
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DEAE-cellulose, GDP-affinity column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
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expression of wild-type and mutant hALG1 in Saccharomyces cerevisiae alg1-1 strain
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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
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C396Y
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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
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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
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the mutation is associated with congenital disorders of glycosylation
M377V
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the mutation is associated with congenital disorders of glycosylation
R276W
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the mutation is associated with congenital disorders of glycosylation
R438W
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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