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G4509

Sigma-Aldrich

Glycerokinase from Escherichia coli

lyophilized powder, 40-100 units/mg protein

Synonyme(s) :

ATP:glycerol 3-phosphotransferase, Glycerol Kinase

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About This Item

Numéro CAS:
9030-66-4
Numéro de classification (Commission des enzymes):
2.7.1.30 (BRENDA, IUBMB)
Numéro CE :
232-862-0
Numéro MDL:
MFCD00131205
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Escherichia coli

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

40-100 units/mg protein

Composition

Protein, ≥50% biuret

Activité étrangère

Triose-phosphate isomerase, hexokinase, myokinase, glycerol dehydrogenase and NADH oxidase ≤0.05%

Température de stockage

−20°C

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Application

Glycerol kinase (glpK) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis.

Actions biochimiques/physiologiques

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>>>

Définition de l'unité

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.

Forme physique

Partially purified lyophilized powder, balance is primarily salts and EDTA.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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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.
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
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
V Van Harmelen et al.
The Journal of biological chemistry, 274(26), 18243-18251 (1999-06-22)
The effects of acylation-stimulating protein (ASP) and insulin on free fatty acid (FFA) release from isolated human fat cells and the signal transduction pathways to induce these effects were studied. ASP and insulin inhibited basal and norepinephrine-induced FFA release by
F Lönnqvist et al.
Arteriosclerosis, thrombosis, and vascular biology, 17(7), 1472-1480 (1997-07-01)
Cardiovascular complications of obesity are more common in men than women. Sex differences in visceral fat lipolysis may be of importance in this respect, since increased release of free fatty acids (FFAs) from visceral fat to the liver by the
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Protocoles

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)

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)

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