Diacylglycerol kinase

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Diacylglycerol kinase
Soluble diacylglycerol kinase DgkB from Staphylococcus aureus.png
DgkB, soluble DAGK from Staphylococcus aureus. α-helices in red, β-strands in yellow, coils in green.
EC number
CAS number 60382-71-0
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Prokaryotic diacylglycerol kinase
Symbol DAGK_prokar
Pfam PF01219
InterPro IPR000829
OPM superfamily 217
OPM protein 2kdc
Diacylglycerol kinase catalytic domain
Symbol DAGK_cat
Pfam PF00781
Pfam clan CL0240
InterPro IPR001206
Diacylglycerol kinase accessory domain
Symbol DAGK_acc
Pfam PF00609
InterPro IPR000756

Diacylglycerol kinase (DGK or DAGK) is a family of enzymes that catalyzes the conversion of diacylglycerol (DAG) to phosphatidic acid (PA), utilizing ATP as a source of the phosphate. In non-stimulated cells, DGK activity is low, allowing DAG to be used for glycerophospholipid biosynthesis, but on receptor activation of the phosphoinositide pathway, DGK activity increases, driving the conversion of DAG to PA. As both lipids are thought to function as bioactive lipid signaling molecules with distinct cellular targets, DGK therefore occupies an important position, effectively serving as a switch by terminating the signalling of one lipid while simultaneously activating signalling by another.[1]

In bacteria, DGK is very small (13 to 15 kD) membrane protein which seems to contain three transmembrane domains.[2] The best conserved region is a stretch of 12 residues which are located in a cytoplasmic loop between the second and third transmembrane domains. Some Gram-positive bacteria also encode a soluble diacylglycerol kinase capable of reintroducing DAG into the phospholipid biosynthesis pathway. DAG accumulates in Gram-positive bacteria as a result of the transfer of glycerol-1-phosphate moieties from phosphatidylglycerol to lipotechoic acid.[3]

Mammalian DGK Isoforms[edit]

Currently, nine members of the DGK family have been cloned and identified. Although all family members have conserved catalytic domains and two cysteine rich domains, they are further classified into five groups according to the presence of additional functional domains and substrate specificity.[4] These are as follows:

  • Type 1 - DGK-α, DGK-β, DGK-γ - contain EF-hand motifs and a recoverin homology domain
  • Type 2 - DGK-δ, DGK-η - contain a pleckstrin homology domain
  • Type 3 - DGK-ε - has specificity for arachidonate-containing DAG
  • Type 4 - DGK-ζ, DGK-ι - contain a MARCKS homology domain, ankyrin repeats, a C-terminal nuclear localisation signal, and a PDZ-binding motif.
  • Type 5 - DGK-θ - contains a third cysteine-rich domain, a pleckstrin homology domain and a proline rich region


  1. ^ Merida I, Avila-Flores A, Merino E (2008). "Diacylglycerol kinases: at the hub of cell signalling". Biochem. J. 409 (1): 1–18. doi:10.1042/BJ20071040. PMID 18062770. 
  2. ^ Smith RL, O'Toole JF, Maguire ME, Sanders CR (September 1994). "Membrane topology of Escherichia coli diacylglycerol kinase". J. Bacteriol. 176 (17): 5459–65. PMC 196734Freely accessible. PMID 8071224. 
  3. ^ Miller DJ, Jerga A, Rock CO, White SW (July 2008). "Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycol kinases". Structure. 16 (7): 1036–46. doi:10.1016/j.str.2008.03.019. PMC 2847398Freely accessible. PMID 18611377. 
  4. ^ Van Blitterswijk, WJ; Houssa, B (2000). "Properties and functions of diacylglycerol kinases". Cellular Signaling. 12 (9–10): 595–605. doi:10.1016/s0898-6568(00)00113-3. PMID 11080611. 

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