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Information on EC 2.7.1.108 - dolichol kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P20048

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Saccharomyces cerevisiae
UNIPROT: P20048 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
dolichol kinase, sec59, atdok1, dolichol phosphokinase, at3g45040, sec59p, dolichol kinase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytidine-5-triphosphate (CTP) dependent dolichol kinase
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dolichol phosphokinase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
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phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:dolichol O-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
71768-07-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + dolichol
CDP + dolichyl phosphate
show the reaction diagram
CTP + dolichol
CDP + dolichyl phosphate
show the reaction diagram
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-
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CTP + dolichol
CDP + dolichyl phosphate
show the reaction diagram
CTP mediated phosphorylation of dolichol, the terminal step in dolichyl monophospate biosynthesis de novo
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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temperature-sensitive Saccharomyces cerevisiae mutants, impaired in dolichol kinase (Sec59p) or dolichyl phosphate mannose synthase (Dpm1p) activity have an aberrant cell wall composition and ultrastructure
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Manually annotated by BRENDA team
Orlowski, J.; Machula, K.; Janik, A.; Zdebska, E.; Palamarczyk, G.
Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions
Yeast
24
239-252
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae SF402-4D
Manually annotated by BRENDA team
Han, G.S.; OHara, L.; Siniossoglou, S.; Carman, G.M.
Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase
J. Biol. Chem.
283
20443-20453
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Juchimiuk, M.; Pasikowska, M.; Zatorska, E.; Laudy, A.E.; Smole?ska-Sym, G.; Palamarczyk, G.
Defect in dolichol-dependent glycosylation increases sensitivity of Saccharomyces cerevisiae towards anti-fungal drugs
Yeast
27
637-645
2010
Saccharomyces cerevisiae (P20048), Saccharomyces cerevisiae
Manually annotated by BRENDA team