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G4509

Sigma-Aldrich

Glycerokinase from Escherichia coli

lyophilized powder, 40-100 units/mg protein

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Synonym(s):
ATP:glycerol 3-phosphotransferase, Glycerol Kinase
CAS Number:
9030-66-4
Enzyme Commission number:
2.7.1.30 (BRENDA, IUBMB)
EC Number:
232-862-0
MDL number:
MFCD00131205
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

200

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

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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>>>

Unit Definition

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.

Physical form

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

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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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
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
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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)

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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