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
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2.7.1.30
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glycerol-3-phosphate
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triglyceride
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adrenal
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hypoplasia
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dystrophy
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muscular
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adipose
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3-phosphate
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duchenne
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lipase
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phosphoenolpyruvate
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hexokinase
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x-linked
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dihydroxyacetone
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contiguous
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adipocytes
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triacylglycerols
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carboxykinase
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congenita
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gluconeogenesis
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glycerophosphate
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lipolysis
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hpr
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iiaglc
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1,6-bisphosphate
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hypogonadism
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co-immobilized
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phosphocarrier
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glyceroneogenesis
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hypogonadotropic
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glycosomes
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dissimilation
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triolein
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1,3-propanediol
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glucose-specific
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aquaglyceroporins
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d-glyceraldehyde
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phosphoenolpyruvate:sugar
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dhap
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phosphoenolpyruvate-dependent
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sn-glycerol-3-phosphate
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sn-glycerol
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drug development
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diagnostics
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synthesis
- 2.7.1.30
- glycerol-3-phosphate
- triglyceride
- adrenal
- hypoplasia
- dystrophy
- muscular
- adipose
- 3-phosphate
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duchenne
- lipase
- phosphoenolpyruvate
- hexokinase
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x-linked
- dihydroxyacetone
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contiguous
- adipocytes
- triacylglycerols
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carboxykinase
- congenita
-
gluconeogenesis
- glycerophosphate
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lipolysis
- hpr
- iiaglc
- 1,6-bisphosphate
- hypogonadism
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co-immobilized
-
phosphocarrier
-
glyceroneogenesis
-
hypogonadotropic
- glycosomes
-
dissimilation
- triolein
- 1,3-propanediol
-
glucose-specific
-
aquaglyceroporins
- d-glyceraldehyde
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phosphoenolpyruvate:sugar
- dhap
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phosphoenolpyruvate-dependent
- sn-glycerol-3-phosphate
- sn-glycerol
- drug development
- diagnostics
- synthesis
Reaction
Synonyms
AFUB_068560, ASTP
ECTree
2.7.1.30 glycerol kinaseAdvanced search results
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results (KM Value
KM Value on EC 2.7.1.30 - glycerol kinase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.24
ADP
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
0.37
ADP
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
0.69
ADP
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
0.095
ATP
enzyme source: crude extract from diapause eggs exposed to 5°C for 200 days, Bombyx mori has 3 glycerol kinase genes
0.32
glycerol
enzyme source: crude extract from diapause eggs exposed to 5°C for 200 days, Bombyx mori has 3 glycerol kinase genes
1.09
sn-glycerol 3-phosphate
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
1.13
sn-glycerol 3-phosphate
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
1.37
sn-glycerol 3-phosphate
in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication
additional information
additional information
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2 Km-values with respect to glycerol may correspond to two different molecular species
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additional information
additional information
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2 Km-values with respect to glycerol may correspond to two different molecular species
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additional information
additional information
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2 Km-values with respect to glycerol may correspond to two different molecular species
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additional information
additional information
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assay at 25°C, increasing pH or decreasing temperature rises Km for glycerol
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additional information
additional information
classical Michaelis-Menten kinetic pattern for the phosphatase reaction
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additional information
additional information
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classical Michaelis-Menten kinetic pattern for the phosphatase reaction
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additional information
additional information
classical Michaelis-Menten kinetic pattern for the phosphatase reaction
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additional information
additional information
Michaelis-Menten kinetics, Tk-GK shows no negative cooperativity for ATP binding, the hexamer formation maintains a high ATP binding affinity
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additional information
additional information
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Michaelis-Menten kinetics, Tk-GK shows no negative cooperativity for ATP binding, the hexamer formation maintains a high ATP binding affinity
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additional information
additional information
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the enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The active site of glycerol kinase shows different catalytic property with respect to different Mg-ATP complexes. Glycerol kinase exhibits high affinity (low Km) and less activity (low kcat) for complexes with a stoichiometric or over-stoichiometric constitution like Mg2+-ATP. On the other hand, the enzyme shows less affinity (high Km) and high activity (high kcat) for unsaturated complexes like [Mg(ATP)2]6-. Detailed kinetic analysis of glycerol kinase as a function of Mg2+ to ATP molar ratio, overview. The enzyme exhibits Michaelis-Menten kinetics. The two-step kinetic behavior of glycerol kinase as function of ATP at a fixed Mg2+ concentration can rather be explained due to the various Mg-ATP complexes formed at different Mg2+/ATP molar ratios that bind to the active site. In consequence, different Km and kcat values are determined with respect to the different Mg-ATP complexes
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