G4509
Glycerokinase from Escherichia coli
lyophilized powder, 40-100 units/mg protein
Synonym(s):
ATP:glycerol 3-phosphotransferase, Glycerol Kinase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-862-0
MDL number:
eCl@ss:
32160410
Specific activity:
40-100 units/mg protein
Biological source:
Escherichia coli
biological source
Escherichia coli
Quality Level
form
lyophilized powder
specific activity
40-100 units/mg protein
composition
Protein, ≥50% biuret
foreign activity
Triose-phosphate isomerase, hexokinase, myokinase, glycerol dehydrogenase and NADH oxidase ≤0.05%
storage temp.
−20°C
Application
Glycerol kinase (glpK) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis.
Biochem/physiol Actions
Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate.
Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. <<<20,21>>> It is also subject to feedback regulation by fructose-1,6-bisphosphate.<<<22>>>
Physical form
Partially purified lyophilized powder, balance is primarily salts and EDTA.
Other Notes
One unit will convert 1.0 μmole of glycerol and ATP to L-α-glycerophosphate and ADP per min at pH 9.8 at 25 °C in a coupled system with PK/LDH.
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Protocols
Enzymatic assay of lipase type XIII from Pseudomonas sp. using a coupled enzyme system of glycerol kinase and glycerophosphate oxidase (EC 3.1.1.3)
Related Content
L Hellström et al.
International journal of obesity and related metabolic disorders : journal of the International Association for the Study of Obesity, 21(4), 314-320 (1997-04-01)
The weight loss achieved during treatment with very-low-calorie diets (VLCD) varies between individuals. The aim of this study was to investigate whether interindividual variations in catecholamine-induced lipolysis are of importance for the rate of weight loss during VLCD. Prospective study.
A Girard et al.
The Biochemical journal, 274 ( Pt 3), 819-824 (1991-03-15)
An artificial-membrane-bound glycerokinase chosen as a membrane-bound two-substrate-enzyme model has been used to separate two unequal compartments of a specially designed diffusion cell. An interesting feature is the asymmetry of compartments and the existence of a diffusion layer adjacent to
S Reynisdottir et al.
Diabetologia, 37(4), 428-435 (1994-04-01)
Upper-body obesity is an important risk factor for developing non-insulin dependent diabetes. To investigate the possibility that a lipolysis defect is present in this form of obesity, we examined the adrenergic regulation of lipolysis in abdominal subcutaneous fat cells from