2.7.1.30: glycerol kinase
This is an abbreviated version!
For detailed information about glycerol kinase, go to the full flat file.
Word Map on EC 2.7.1.30
-
2.7.1.30
-
glycerol-3-phosphate
-
triglyceride
-
adrenal
-
hypoplasia
-
dystrophy
-
muscular
-
adipose
-
3-phosphate
-
duchenne
-
lipase
-
phosphoenolpyruvate
-
hexokinase
-
x-linked
-
dihydroxyacetone
-
contiguous
-
adipocytes
-
triacylglycerols
-
carboxykinase
-
congenita
-
gluconeogenesis
-
glycerophosphate
-
lipolysis
-
hpr
-
iiaglc
-
1,6-bisphosphate
-
hypogonadism
-
co-immobilized
-
phosphocarrier
-
glyceroneogenesis
-
hypogonadotropic
-
glycosomes
-
dissimilation
-
triolein
-
1,3-propanediol
-
glucose-specific
-
aquaglyceroporins
-
d-glyceraldehyde
-
phosphoenolpyruvate:sugar
-
dhap
-
phosphoenolpyruvate-dependent
-
sn-glycerol-3-phosphate
-
sn-glycerol
-
drug development
-
diagnostics
-
synthesis
- 2.7.1.30
- glycerol-3-phosphate
- triglyceride
- adrenal
- hypoplasia
- dystrophy
- muscular
- adipose
- 3-phosphate
-
duchenne
- lipase
- phosphoenolpyruvate
- hexokinase
-
x-linked
- dihydroxyacetone
-
contiguous
- adipocytes
- triacylglycerols
-
carboxykinase
- congenita
-
gluconeogenesis
- glycerophosphate
-
lipolysis
- hpr
- iiaglc
- 1,6-bisphosphate
- hypogonadism
-
co-immobilized
-
phosphocarrier
-
glyceroneogenesis
-
hypogonadotropic
- glycosomes
-
dissimilation
- triolein
- 1,3-propanediol
-
glucose-specific
-
aquaglyceroporins
- d-glyceraldehyde
-
phosphoenolpyruvate:sugar
- dhap
-
phosphoenolpyruvate-dependent
- sn-glycerol-3-phosphate
- sn-glycerol
- drug development
- diagnostics
- synthesis
Reaction
Synonyms
AFUB_068560, ASTP
ECTree
Advanced search results
Subunits
Subunits on EC 2.7.1.30 - glycerol kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
dimer or tetramer
-
2 or 4 * 60000, in solution, the enzyme exists in a dimer-tetramer equilibrium
hexamer
homodimer
homotetramer
dimer-tetramer equilibrium in solution, tetramer in the crystal
tetramer
additional information
dimer
light scattering analysis confirmed G230D is a dimer and is resistant to tetramer formation in the presence of fructose 1,6-bisphosphate, whereas the wild type enzyme dimers are converted into putatively inactive tetramers in the presence of fructose 1,6-bisphosphate.
dimer
-
Tk-GK is a dimer in solution in absence of glycerol
-
Tk-GK has a hexameric form with a threefold axis in the crystal lattice
hexamer
-
Tk-GK has a hexameric form with a threefold axis in the crystal lattice
-
hexamer
-
Tk-GK has a hexameric form with a threefold axis in the crystal lattice
-
homodimer
2 x 57289 (501 residues plus an additional six N-terminal residues from the linker region), mass spectrometry
tetramer
-
4 * 55000-57000, equilibrium ultracentrifugation in presence of 6 M guanidine HCl, SDS-PAGE
in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
additional information
-
in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
additional information
-
in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
-
additional information
-
in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
-