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Information on EC 2.7.1.108 - dolichol kinase and Organism(s) Homo sapiens and UniProt Accession Q9UPQ8
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2.7.1.108 dolichol kinaseSpecify your search results
Word Map
- 2.7.1.108
- dolichyl
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n-glycosylation
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ctp-dependent
- polyprenols
- cis-prenyltransferase
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dolichol-linked
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mannosylated
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o-mannosylation
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polyisoprenoids
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pyrophosphorylated
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alpha-isoprene
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
dolichol kinase, sec59, atdok1, dolichol phosphokinase, at3g45040, sec59p, dolichol kinase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dolichol phosphokinase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
CTP:dolichol O-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
71768-07-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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the chain length of eukaryotic dolichol molecules is species specific and differs from 14-17 isoprene units in unicellular organisms like the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, mammalian cells produce longer dolichol molecules with 18-21 isoprene units
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-
?
CTP + dolichol
CDP + dolichyl phosphate
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CTP mediated phosphorylation of dolichol, the terminal step in dolichyl monophospate biosynthesis de novo
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?
CTP + dolichol
CDP + dolichyl phosphate
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DK1 is responsible for the final step of the de novo biosynthesis of dolichol phosphate
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-
?
CTP + dolichol
CDP + dolichyl phosphate
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a defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
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-
?
CTP + dolichol
CDP + dolichyl phosphate
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DK1 is responsible for the final step of the de novo biosynthesis of dolichol phosphate, defect in human DK1 affects the biosynthesis of dolichol phosphate by the disturbance of the final phosphorylation step, causes lethal phenotype with death in early infancy.
dolichyl phosphate is involved in several glycosylation reactions, such as N-glycosylation, glycosylphosphatidylinositol (GPI)-anchor biosynthesis, and C- and O-mannosylation
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the chain length of eukaryotic dolichol molecules is species specific and differs from 14-17 isoprene units in unicellular organisms like the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, mammalian cells produce longer dolichol molecules with 18-21 isoprene units
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
CTP mediated phosphorylation of dolichol, the terminal step in dolichyl monophospate biosynthesis de novo
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
DK1 is responsible for the final step of the de novo biosynthesis of dolichol phosphate
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
DK1 is responsible for the final step of the de novo biosynthesis of dolichol phosphate, defect in human DK1 affects the biosynthesis of dolichol phosphate by the disturbance of the final phosphorylation step, causes lethal phenotype with death in early infancy.
dolichyl phosphate is involved in several glycosylation reactions, such as N-glycosylation, glycosylphosphatidylinositol (GPI)-anchor biosynthesis, and C- and O-mannosylation
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
extracts gained from patient fibroblasts show remarkably lower enzyme activity than extracts from control cells, in comparison with controls, the decrease in activity was 94.5-98.6% for all patients
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
polytopic membrane protein localized in the endoplasmic reticulum with an N-terminus extended into the lumen and a cytoplasmically oriented C-terminus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
human DOLK deficiency, also known as DOLK-CDG or CDG-Im, results in a syndrome that manifests with dilated cardiomyopathy of variable severity, phenotype with dysmorphic features, genital abnormalities, talipes equinovarus, and severe, refractory generalized seizures. Additional multi-systemicmanifestations develop including dilated cardiomyopathy, hepatomegaly, severe insulin-resistant hyperglycemia, and renal failure, which are ultimately fatal in the first months
metabolism
the enzyme catalyzing the final step in the biosynthesis of dolichol phosphate
physiological function
dolichol kinase catalyzes the final step in biosynthesis of dolichol phosphate, which is the oligosaccharide carrier required for protein N-glycosylation
malfunction
metabolism
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dolichol metabolim, the enzymatic product dolichyl phosphate is a lipid carrier embedded in the endoplasmic reticulum membrane essential for the synthesis of N-glycans, GPI-anchors and protein C- and O-mannosylation
malfunction
-
a deficiency of dolichol kinase, catalyzing the final step of dolichol phosphate synthesis is the first defect of the dolichyl phosphate pathway known to cause a severe hypoglycosylation phenotype in humans, length, weight and head circumference are normal at birth but secondary microcephaly, developing in the first month of life is a common finding in all patients
malfunction
-
identifikation of 4 patients who are homozygous for one of 2 mutations (C99S and Y441S) in the corresponding hDK1 gene, the residual activity of mutant is 2-4% when compared with control cells, the mutated alleles fail to complement the temperature-sensitive phenotype of dolichol kinase-deficient yeast cells, whereas the wild-type allele restores the normal growth phenotype, affected patients present with a very severe clinical phenotype, with death in early infancy, 2 of the patients died from dilative cardiomyopathy
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DOLK_HUMAN
538
14
59268
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q483K
naturally occuring homozygous c.1447C>A DOLK mutation involved in enzyme deficiency and a phenotype with anatomic malformations and multi-systemic dysfunction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
human cDNA complements defect in dolichol kinase activity in Saccharomyces cerevisiae sec59-1 mutant, human SEC59 gene also expressed in Sf-9 cells
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overexpression of normal or variant forms of hDK in CHO cells and in yeast sec59-1 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandez, F.; Shridas, P.; Jiang, S.; Aebi, M.; Waechter, C.J.
Expression and characterization of a human cDNA that complements the temperature-sensitive defect in dolichol kinase activity in the yeast sec59-1 mutant: the enzymatic phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated kinase activities in Saccharomyces cerevisiae
Glycobiology
12
555-562
2002
Homo sapiens, Saccharomyces cerevisiae (P20048), Saccharomyces cerevisiae
Kranz, C.; Jungeblut, C.; Denecke, J.; Erlekotte, A.; Sohlbach, C.; Debus, V.; Kehl, H.G.; Harms, E.; Reith, A.; Reichel, S.; Grbe, H.; Hammersen, G.; Schwarzer, U.; Marquardt, T.
A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
Am. J. Hum. Genet.
80
433-440
2007
Homo sapiens
Shridas, P.; Waechter, C.J.
Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site
J. Biol. Chem.
281
31696-31704
2006
Homo sapiens
Denecke, J.; Kranz, C.
Hypoglycosylation due to dolichol metabolism defects
Biochim. Biophys. Acta
1792
888-895
2009
Homo sapiens
Lieu, M.T.; Ng, B.G.; Rush, J.S.; Wood, T.; Basehore, M.J.; Hegde, M.; Chang, R.C.; Abdenur, J.E.; Freeze, H.H.; Wang, R.Y.
Severe, fatal multisystem manifestations in a patient with dolichol kinase-congenital disorder of glycosylation
Mol. Genet. Metab.
110
484-489
2013
Homo sapiens (Q9UPQ8), Homo sapiens
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