2.7.1.108: dolichol kinase
This is an abbreviated version!
For detailed information about dolichol kinase, go to the full flat file.
Word Map on EC 2.7.1.108
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2.7.1.108
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dolichyl
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n-glycosylation
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ctp-dependent
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polyprenols
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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
- 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
Reaction
Synonyms
At3g45040, AtDOK1, cytidine-5-triphosphate (CTP) dependent dolichol kinase, DK, DK1, DOK1, dolichol kinase, dolichol kinase 1, dolichol phosphokinase, dolichol-specific kinase, DOLK, SEC59, Sec59p
ECTree
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General Information
General Information on EC 2.7.1.108 - dolichol kinase
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malfunction
metabolism
physiological function
additional information
AtDOK1 contains a DxxAxxxGxxxGx8KKTxEG motif that is conserved among enzymes utilizing CTP as a substrate, including hDOLK and yeast Sec59p. The motif contains the CTP binding site
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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
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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
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
malfunction
the heterozygous T-DNA-tagged AtDOK1 mutant, dok1-1 and dok1-2, plants show developmental defects in male and female gametophytes, including an aberrant pollen structure, low pollen viability, and short siliques. Additionally, the mutations has incomplete penetrance. Mutation of dok-1 may affect development of siliques but not seed maturation or germination in Arabidopsis thaliana. Male gametophytic defect in dok1 heterozygous plants, overview
malfunction
two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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malfunction
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two mutations in the Kluyveromyces lactis KlSEC59 gene, encoding dolichol kinase (DK), are responsible for an enhanced secretion phenotype in the previously isolated mutant, MD2/1-9. Compared with the temperature-sensitive Saccharomyces cerevisiae sec59-1 mutant, which exhibits reduced N-glycosylation and decreased secretory efficacy, the identified Kluyveromyces lactis DK mutations has fewer effects on glycosylation, as well as on survival at high temperature and cell wall integrity. Mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype. Despite some glycosylation defects, double DK mutations (G405S/I419S) in the Kluyveromyces lactis mutant strain demonstrate three times the level of recombinant alpha-amylase secretion compared to wild-type strain. Overexpression of potential suppressors KlMNN10, KlSEL1, KlERG20, KlSRT1, KlRER2, KlCAX4, KlLPP1 and KlDPP1 in the DK-mutant strain restores carboxypeptidase Y glycosylation to different extents and, with the exception of KISRT1, reduces alpha-amylase secretion to levels observed in wild-type cells. The mutant strain shows substantial reduction of protein N-glycosylation, secretion efficacy, and growth rate, particularly at the nonpermissive temperature
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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
metabolism
the enzyme catalyzing the final step in the biosynthesis of dolichol phosphate
a strain impaired in dolichol kinase function shows aberrant cell wall structure and composition. the strain is resistant to itraconazole, but sensitive to 5-fluorocytosine, amphotericin B, caspofungin. The minimal inhibitory concentration of caspofungin and amphotericin B is 2fold lower for the mutant than for the respective wild-type strain. The sensitivity of the mutant can be brought back to the wild-type level by a multicopy suppressor of the thermosensitive phenotype, the RER2 gene, encoding cis-prenyltransferase involved in dolichol biosynthesis
physiological function
dolichol kinase catalyzes the final step in biosynthesis of dolichol phosphate, which is the oligosaccharide carrier required for protein N-glycosylation
physiological function
the enzyme is required for reproductive processes in Arabidopsis thaliana
physiological function
Arabidopsis thaliana dolichol kinase 1, AtDOK1, is functionally involved in plant reproductive processes. Dolichols are a class of isoprenoids that consist of highly polymerized and unsaturated long-chain isoprenes. They play crucial roles in protein glycosylation including N-glycosylation, because the oligosaccharide is assembled on a lipid carrier, dolichyl diphosphate. Dolichol phosphate mannose (Dol-P-Man) serves as a lipid carrier for the initial steps of N-glycosylation, O-mannosylation, and glycosylphosphatidylinositol (GPI) anchoring. The endoplasmic reticulum-localized catalytically active DOK1 is highly expressed in the meristems and is involved in the control of flowering time, possibly by post-transcriptional regulation including protein glycosylation. DOK1 may post-transcriptionally affect factors that regulate flowering time control because DOK is involved in protein glycosylation, including N-glycosylation, O-mannosylation, and GPI anchoring