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CTP + dolichol
CDP + dolichyl phosphate
CTP + ficaprenol
CDP + ficaprenyl phosphate
CTP + polyprenol
CDP + polyprenyl phosphate
dCTP + dolichol
dCDP + dolichyl phosphate
-
-
-
?
additional information
?
-
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
newly formed dolichyl monophosphate, phosphorylated via CTP is available for biosynthesis of mannosylphosphoryldolichol and N-acetylglucosaminylpyrophosphoryldolichol
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
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
-
a defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
-
-
?
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
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
pig liver dolichol as substrate, R,S-dolichol-11, dolichol-16, dolichol-19
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
enzyme can function in augmenting the steady-state levels of dolichyl phosphate by phosphorylating preexisting dolichol molecules
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
pig liver dolichol as substrate, R,S-dolichol-11, dolichol-16, dolichol-19
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
enzyme can function in augmenting the steady-state levels of dolichyl phosphate by phosphorylating preexisting dolichol molecules
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
CTP mediated phosphorylation of dolichol, the terminal step in dolichyl monophospate biosynthesis de novo
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
-
?
CTP + dolichol
CDP + dolichyl phosphate
-
-
-
?
CTP + ficaprenol
CDP + ficaprenyl phosphate
-
-
-
-
?
CTP + ficaprenol
CDP + ficaprenyl phosphate
-
-
-
-
?
CTP + polyprenol
CDP + polyprenyl phosphate
-
polyprenol-16, alpha-trans-polyprenol-16, polyprenol-19
-
-
?
CTP + polyprenol
CDP + polyprenyl phosphate
-
polyprenol-16, alpha-trans-polyprenol-16, polyprenol-19
-
-
?
additional information
?
-
-
ATP and GTP are not effective substrates compared to CTP
-
-
?
additional information
?
-
-
CTP or other phosphate group donors like ATP, GTP or UTP are not required for maximal activity
-
-
?
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
-
-
?
additional information
?
-
-
requires CTP as phosphoryl donor
-
-
?
additional information
?
-
-
ATP cannot replace CTP
-
-
?
additional information
?
-
-
microsomal enzyme shows a marked preference for saturation of the alpha-isoprene, dolichol-16 and dolichol-19 are 2.5fold more active than the corresponding polyprenols, the enzyme is twice as active against naturally occurring polyprenol-16 (alpha-cis-isoprene) compared to synthetic alpha-trans-polyprenol-16, all-trans-2,3-dihydrosolanesol and solanesol are not substrates
-
-
?
additional information
?
-
-
microsomal enzyme shows a marked preference for saturation of the alpha-isoprene, dolichol-16 and dolichol-19 are 2.5fold more active than the corresponding polyprenols, the enzyme is twice as active against naturally occurring polyprenol-16 (alpha-cis-isoprene) compared to synthetic alpha-trans-polyprenol-16, all-trans-2,3-dihydrosolanesol and solanesol are not substrates
-
-
?
additional information
?
-
-
requires CTP as phosphoryl donor
-
-
?
additional information
?
-
-
ATP cannot replace CTP
-
-
?
additional information
?
-
-
ATP, UTP and GTP are ineffective
-
-
?
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Carcinoma, Hepatocellular
Cytidine 5'-triphosphate-dependent dolichol kinase and dolichol phosphatase activities and levels of dolichyl phosphate in microsomal fractions from highly differentiated human hepatomas.
Cardiomyopathy, Dilated
From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG).
Congenital Disorders of Glycosylation
From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG).
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG).
Cysts
Dolichol phosphorylation occurs via a CTP-dependent reaction in Artemia larvae.
dolichol kinase deficiency
Autosomal recessive dilated cardiomyopathy due to DOLK mutations results from abnormal dystroglycan O-mannosylation.
dolichol kinase deficiency
Dolichol kinase deficiency (DOLK-CDG) with a purely neurological presentation caused by a novel mutation.
dolichol kinase deficiency
Dolichol kinase deficiency (DOLK-CDG): Two new cases and expansion of phenotype.
dolichol kinase deficiency
Fatal hyperkeratosis syndrome in four siblings due to dolichol kinase deficiency.
dolichol kinase deficiency
From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG).
Intestinal Volvulus
Dolichol kinase in Ascaris suum and Onchocerca volvulus.
Neoplasms
Cytidine 5'-triphosphate-dependent dolichol kinase and dolichol phosphatase activities and levels of dolichyl phosphate in microsomal fractions from highly differentiated human hepatomas.
Nervous System Diseases
A forward genetic screen identifies Dolk as a regulator of startle magnitude through the potassium channel subunit Kv1.1.
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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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
metabolism
-
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
physiological function
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
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G471D
site-directed mutagenesis,inactive mutant
Q483K
naturally occuring homozygous c.1447C>A DOLK mutation involved in enzyme deficiency and a phenotype with anatomic malformations and multi-systemic dysfunction
G405S
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
G405S/I419S
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
I419S
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
G405S/I419S
-
site-directed mutagenesis, despite some glycosylation defects, double DK mutations (G405S and 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
-
I419S
-
naturally occuring mutation, identified in the isolated mutant strain MD2/1-9, the mutation leads to reduced dolichol kinase activity and the enhanced secretion phenotype
-
W332G
-
mutated Sec59-1p bears the single amino acid substitution Trp(332) to Gly, region predicted to be responsible for the substrate (dolichol) binding
W332G
-
mutated Sec59-1p bears the single amino acid substitution Trp(332) to Gly, region predicted to be responsible for the substrate (dolichol) binding
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additional information
construction of two independent lines of T-DNA-tagged AtDOK1 mutants, designated dok1-1 (CS822420; SAIL_529_E06) and dok1-2 (CS856101; WiscDsLox443D6), with T-DNA insertions in exons 8 and 13, respectively. Mutant dok1-1/+ and wild-type seed morphologies show no significant differences, and dok1-1/+ and the wild type did not differ in seed germination rates
additional information
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construction of two independent lines of T-DNA-tagged AtDOK1 mutants, designated dok1-1 (CS822420; SAIL_529_E06) and dok1-2 (CS856101; WiscDsLox443D6), with T-DNA insertions in exons 8 and 13, respectively. Mutant dok1-1/+ and wild-type seed morphologies show no significant differences, and dok1-1/+ and the wild type did not differ in seed germination rates
additional information
creation of leaky knockdown mutants of gene DOK1 by microRNA-mediated gene suppression technique. Knockout of gene DOK1 causes lethality, while the DOK1 knockdown mutants show an early flowering phenotype without any remarkable growth defect in vegetative tissues
additional information
phenotypic characterization of CBS2359-KlSEC59 mutants, overview
additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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additional information
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phenotypic characterization of CBS2359-KlSEC59 mutants, overview
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19
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Kluyveromyces lactis (Q6CR79), Kluyveromyces lactis, Kluyveromyces lactis CBS 2359 (Q6CR79), Kluyveromyces lactis NRRL Y-1140 (Q6CR79), Kluyveromyces lactis DSM 70799 (Q6CR79), Kluyveromyces lactis WM37 (Q6CR79), Kluyveromyces lactis ATCC 8585 (Q6CR79), Kluyveromyces lactis NBRC 1267 (Q6CR79)
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Arabidopsis thaliana (F4J4C8)
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