In enzymology, a dolichol kinase (EC 2.7.1.108) is an enzyme that catalyzes the chemical reaction

dolichol kinase
Identifiers
EC no.2.7.1.108
CAS no.71768-07-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
DOLK
Identifiers
AliasesDOLK, CDG1M, DK, DK1, SEC59, TMEM15, dolichol kinase
External IDsOMIM: 610746; MGI: 2677836; HomoloGene: 8940; GeneCards: DOLK; OMA:DOLK - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_014908

NM_177648

RefSeq (protein)

NP_055723

NP_808316

Location (UCSC)Chr 9: 128.95 – 128.95 MbChr 2: 30.17 – 30.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
CTP + dolichol CDP + dolichyl phosphate

Thus, the two substrates of this enzyme are CTP and dolichol, whereas its two products are CDP and dolichyl phosphate.

This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase. This enzyme participates in N-glycan biosynthesis.

In humans dolichol kinase is encoded by the DOLK gene.[5][6][7]

Function

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Dolichyl monophosphate is an essential glycosyl carrier lipid for C- and O-mannosylation and N-glycosylation of proteins and for biosynthesis of glycosylphosphatidylinositol anchors in endoplasmic reticulum (ER). Dolichol kinase catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate biosynthesis.[8]

Clinical significance

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Mutations in DOLK cause a subtype of the congenital disorders of glycosylation, DOLK-CDG (CDG-Im).[9]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175283Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000075419Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A (Oct 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  6. ^ Shridas P, Waechter CJ (Oct 2006). "Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with a cytoplasmically oriented CTP-binding site". J Biol Chem. 281 (42): 31696–704. doi:10.1074/jbc.M604087200. PMID 16923818.
  7. ^ "Entrez Gene: DOLK dolichol kinase".
  8. ^ Fernandez F, Shridas P, Jiang S, Aebi M, Waechter CJ (September 2002). "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" (PDF). Glycobiology (Submitted manuscript). 12 (9): 555–62. doi:10.1093/glycob/cwf068. PMID 12213788.
  9. ^ Kranz C, Jungeblut C, Denecke J, Erlekotte A, Sohlbach C, Debus V, Kehl HG, Harms E, Reith A, Reichel S, Grobe H, Hammersen G, Schwarzer U, Marquardt T (March 2007). "A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy". Am. J. Hum. Genet. 80 (3): 433–40. doi:10.1086/512130. PMC 1821118. PMID 17273964.

Further reading

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