Dolichol kinase

dolichol kinase
Identifiers
EC number	2.7.1.108
CAS number	71768-07-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

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

CTP + dolichol <math>\rightleftharpoons</math> 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.

Function

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.

Clinical significance

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

See also

• Dolichol kinase deficiency

Further reading

• Burton WA, Scher MG, Waechter CJ (1979). "Enzymatic phosphorylation of dolichol in central nervous tissue". J. Biol. Chem. 254 (15): 7129&ndash, 36. PMID 457672.
• Rip JW, Carroll KK (1980). "Properties of a dolichol phosphokinase activity associated with rat liver microsomes". Can. J. Biochem. 58 (10): 1051&ndash, 6. doi:10.1139/o80-142. PMID 6257336.
• Kranz C, Jungeblut C, Denecke J, et al. (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.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kikuno R, Nagase T, Ishikawa K, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview