ジアシルグリセロールキナーゼ
WordNet
- an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
- the basic unit of money in Papua New Guinea
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/07/04 02:46:03」(JST)
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Diacylglycerol kinase |
DgkB, soluble DAGK from Staphylococcus aureus. α-helices in red, β-strands in yellow, coils in green.
|
Identifiers |
EC number |
2.7.1.107 |
CAS number |
60382-71-0 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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Prokaryotic diacylglycerol kinase |
Identifiers |
Symbol |
DAGK_prokar |
Pfam |
PF01219 |
InterPro |
IPR000829 |
PROSITE |
PDOC00820 |
OPM superfamily |
217 |
OPM protein |
2kdc |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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Diacylglycerol kinase catalytic domain |
Identifiers |
Symbol |
DAGK_cat |
Pfam |
PF00781 |
Pfam clan |
CL0240 |
InterPro |
IPR001206 |
SMART |
DAGKc |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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Diacylglycerol kinase accessory domain |
Identifiers |
Symbol |
DAGK_acc |
Pfam |
PF00609 |
InterPro |
IPR000756 |
SMART |
DAGKa |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
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
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
References
- ^ Merida I, Avila-Flores A, Merino E (2008). "Diacylglycerol kinases: at the hub of cell signalling.". Biochem. J. 409 (1): 1–18. PMID 18062770. doi:10.1042/BJ20071040.
- ^ 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 196734 . PMID 8071224.
- ^ 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. PMC 2847398 . PMID 18611377. doi:10.1016/j.str.2008.03.019.
- ^ Van Blitterswijk, WJ; Houssa, B (2000). "Properties and functions of diacylglycerol kinases.". Cellular Signaling. 12 (9–10): 595–605. PMID 11080611. doi:10.1016/s0898-6568(00)00113-3.
External links
- Diacylglycerol Kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 2.7.1.107
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Anabolism |
- to diacylglycerol: Acyltransferase
- Phosphatidate phosphatase
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- Choline kinase
- Choline-phosphate cytidylyltransferase
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- phosphatidylinositol glycan anchor biosynthesis:
- PIGA
- PIGB
- PIGC
- PIGF
- PIGG
- PIGH
- PIGK
- PIGL
- PIGM
- PIGN
- PIGO
- PIGP
- PIGQ
- PIGS
- PIGT
- PIGU
- PIGV
- PIGW
- PIGX
- PIGY
- PIGZ
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Catabolism |
|
- Diacylglycerol kinase
- DGKA
- DGKB
- DGKD
- DGKE
- DGKG
- DGKH
- DGKI
- DGKK
- DGKQ
- DGKZ
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- Phosphoric monoester hydrolases
- Inositol-phosphate phosphatase
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Transferases: phosphorus-containing groups (EC 2.7)
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2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
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2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate kinase
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2.7.3: N acceptor |
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2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
|
|
2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
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2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
Polymerase |
DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
|
RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
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Phosphorolytic
3' to 5' exoribonuclease |
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Nucleotidyltransferase |
- UTP—glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
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Guanylyltransferase |
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Other |
- Recombinase (Integrase)
- Transposase
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2.7.8: miscellaneous |
Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
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Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
|
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2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
2.7.10: protein-tyrosine |
|
2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
|
2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
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2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
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Enzymes
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- Comparative analysis of the hepatopancreas transcriptome of grass carp (Ctenopharyngodon idellus) fed with lard oil and fish oil diets.
- Tian JJ1, Lu RH2, Ji H3, Sun J1, Li C1, Liu P1, Lei CX1, Chen LQ4, Du ZY4.
- Gene.Gene.2015 Jul 10;565(2):192-200. doi: 10.1016/j.gene.2015.04.010. Epub 2015 Apr 10.
- n-3 highly unsaturated fatty acids (n-3 HUFAs) have been shown to suppress lipid accumulation and improve protein utilization in grass carp; however, little is known about the underlying molecular mechanism. Hence, we analyzed the hepatopancreas transcriptome of grass carp (Ctenopharyngodon idellus)
- PMID 25865300
- Protein kinase D1/2 is involved in the maturation of multivesicular bodies and secretion of exosomes in T and B lymphocytes.
- Mazzeo C1, Calvo V1, Alonso R1, Mérida I2, Izquierdo M1.
- Cell death and differentiation.Cell Death Differ.2015 Jun 5. doi: 10.1038/cdd.2015.72. [Epub ahead of print]
- Multivesicular bodies (MVBs) are endocytic compartments that enclose intraluminal vesicles (ILVs) formed by inward budding from the limiting membrane of endosomes. In T lymphocytes, these ILV contain Fas ligand (FasL) and are secreted as 'lethal exosomes' following activation-induced fusion of the M
- PMID 26045048
- Characterization of a New DGKE Intronic Mutation in Genetically Unsolved Cases of Familial Atypical Hemolytic Uremic Syndrome.
- Mele C1, Lemaire M1, Iatropoulos P1, Piras R1, Bresin E1, Bettoni S1, Bick D1, Helbling D1, Veith R1, Valoti E1, Donadelli R1, Murer L1, Neunhäuserer M1, Breno M1, Frémeaux-Bacchi V1, Lifton R1, Remuzzi G2, Noris M1.
- Clinical journal of the American Society of Nephrology : CJASN.Clin J Am Soc Nephrol.2015 Jun 5;10(6):1011-9. doi: 10.2215/CJN.08520814. Epub 2015 Apr 8.
- BACKGROUND AND OBJECTIVES: Genetic and acquired abnormalities causing dysregulation of the complement alternative pathway contribute to atypical hemolytic uremic syndrome (aHUS), a rare disorder characterized by thrombocytopenia, nonimmune microangiopathic hemolytic anemia, and acute kidney failure.
- PMID 25854283
Japanese Journal
- Diacylglycerol Signaling Pathway in Pancreatic β-Cells : An Essential Role of Diacylglycerol Kinase in the Regulation of Insulin Secretion (Recent Progress in the Research of Insulin Secretion)
- Kaneko Yukiko K.,Ishikawa Tomohisa
- Biological & pharmaceutical bulletin 38(5), 669-673, 2015-05
- NAID 40020440656
- Diacylglycerol Signaling Pathway in Pancreatic β-Cells: An Essential Role of Diacylglycerol Kinase in the Regulation of Insulin Secretion
- Kaneko Yukiko K.,Ishikawa Tomohisa
- Biological and Pharmaceutical Bulletin 38(5), 669-673, 2015
- … Diacylglycerol (DAG) is a lipid signal messenger and plays a physiological role in β-cells. … Although the primary function of DAG is to activate protein kinase C (PKC), the role of PKC in insulin secretion is controversial: PKC has been reported to act as both a positive and negative regulator of insulin secretion. … The intracellular levels of DAG are strictly regulated by diacylglycerol kinase (DGK); …
- NAID 130005068090
- 吉田 瑶子,松本 雅則
- 臨床血液 56(2), 185-193, 2015
- 非典型溶血性尿毒症症候群(aHUS)は,微小血管症性溶血性貧血,血小板減少,急性腎障害の3徴候で知られている希少疾患である。aHUSという病名は,志賀毒素産生大腸菌(STEC)感染HUSと区別するために使用されてきた。aHUSの多くの症例(約70%)で,補体活性化第二経路に属する因子の遺伝子異常が報告されている。また,最近では凝固関連因子異常がaHUSの病因であることも示されたが,本稿では補体関連 …
- NAID 130004920707
★リンクテーブル★
[★]
キナーゼ カイネース リン酸化酵素 phosphoenzyme phosphotransferase
[★]
ジアシルグリセロール。DG DAG