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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Engineering
Engineering on EC 2.7.1.108 - dolichol kinase
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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
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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
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G405S/I419S
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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
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I419S
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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
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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
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I419S
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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
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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
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I419S
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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
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W332G
additional information
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mutated Sec59-1p bears the single amino acid substitution Trp(332) to Gly, region predicted to be responsible for the substrate (dolichol) binding
W332G
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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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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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