Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.107 - diacylglycerol kinase (ATP) and Organism(s) Staphylococcus aureus and UniProt Accession Q6GFF9

for references in articles please use BRENDA:EC2.7.1.107
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus aureus
UNIPROT: Q6GFF9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dgk, diacylglycerol kinase, dag kinase, dg kinase, dgkzeta, dagk, dgkalpha, dgk-zeta, diglyceride kinase, dgkepsilon, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,2-diacylglycerol kinase
-
-
-
-
adenosine 5'-triphosphate:1,2-diacylglycerol 3-phosphotransferase
-
-
-
-
arachidonoyl-specific diacylglycerol kinase
-
-
-
-
ATP:diacylglycerol phosphotransferase
-
-
-
-
DAGK
-
-
-
-
DAGKalpha
-
-
-
-
DG kinase
-
-
-
-
DGK
-
-
-
-
DGK-alpha
-
-
-
-
DGK-theta
-
-
-
-
DGKbeta
-
-
-
-
DGKdelta
-
-
-
-
DGKgamma
-
-
-
-
DGKiota
-
-
-
-
DGKksi
-
-
-
-
diacylglycerol kinase
-
-
-
-
diacylglycerol kinase (ATP dependent)
-
-
-
-
diacylglycerol:ATP kinase
-
-
-
-
diglyceride kinase
-
-
-
-
kinase (phosphorylating), 1,2-diacylglycerol
-
-
-
-
kinase, 1,2-diacylglycerol (phosphorylating)
-
-
-
-
sn-1,2-diacylglycerol kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
CAS REGISTRY NUMBER
COMMENTARY hide
60382-71-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
1,2-diacylglycerol embedded in unilamellar dioleoyl-phosphatidylcholine vesicles is not a substrate for DgkB
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dioleoyl-phosphatidylglycerol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
0.0023
mutant enzyme N96A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0024
mutant enzyme D124A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0028
mutant enzyme K15A/K165A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0031
mutant enzyme T94A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0036
mutant enzyme D97A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0062
mutant enzyme D216A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0122
mutant enzyme K15A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0139
mutant enzyme K165A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0168
mutant enzyme R100A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0249
wild type enzyme, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
0.0256
mutant enzyme R20A, in 50 mM HEPES, pH 7.4, 150 mM LiCl, 10 mM MgCl2, 5 mM ATP, and lipid vesicles
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37333
x * 37333, calculated, x * 42000, SDS-PAGE
42000
x * 37333, calculated, x * 42000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37333, calculated, x * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform DgkB, both as free enzyme and in complex with ADP, 2.4 and 2.3 A resolution, respectively. Enzyme is a tight homodimer, and each monomer comprises two domains with the catalytic center located within the interdomain cleft
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D124A
D216A
mutant shows strongly reduced activity
D271A
D97A
mutant shows strongly reduced activity
E273A
K15A
mutant shows reduced activity
K15A/K165A
mutant shows strongly reduced activity
K165A
mutant shows reduced activity
N96A
mutant shows strongly reduced activity
R100A
mutant shows reduced activity
R20A
mutant shows wild type activity
T94A
mutant shows strongly reduced activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miller, D.J.; Jerga, A.; Rock, C.O.; White, S.W.
Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases
Structure
16
1036-1046
2008
Staphylococcus aureus (Q6GFF9), Staphylococcus aureus
Manually annotated by BRENDA team
Jerga, A.; Miller, D.J.; White, S.W.; Rock, C.O.
Molecular determinants for interfacial binding and conformational change in a soluble diacylglycerol kinase
J. Biol. Chem.
284
7246-7254
2009
Staphylococcus aureus (Q6GFF9)
Manually annotated by BRENDA team