G6142
Glycerokinase from Cellulomonas sp.
lyophilized powder, 25-75 units/mg protein
Synonym(s):
glpK, ATP:glycerol 3-phosphotransferase, Glycerol Kinase
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About This Item
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form
lyophilized powder
Quality Level
specific activity
25-75 units/mg protein
mol wt
~128 kDa (by gel filtration)
composition
Protein, ≥60% biuret
storage temp.
−20°C
General description
Research area: Cell Signaling
Glycerol kinase (GK) is part of the FGGY carbohydrate kinase family.
Glycerol kinase (GK) is part of the FGGY carbohydrate kinase family.
Application
Glycerokinase from Cellulomonas sp. has been used:
- for determining the kinetic characteristics of human and trypanosomatid phosphofructokinases using an enzyme-linked kinetic assay.
- to study the effect of sugar in fluorescence emission.
- in 2-Arachidonoylglycerol-based fluorescence assay for DH-463, a fluorescent activity-based probe for monoacylglycerol lipase.
Biochem/physiol Actions
Glycerol kinase catalyzes the 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.Mutations in this gene are associated with Glycerol Kinase Deficiency (GKD), a condition characterized primarily by hypertriglyceridemia and hypoglycemia. This enzyme is useful for enzymatic determination of glycerol and triglyceride when coupled with glycerol-3-phosphate dehydrogenase (=G-3-P DH, G3D-301), glycerol-3-phosphate oxidase (=G-3-P oxidase, G3O-301, G3O-311, G3O-321) or pyruvate kinase (PYK-301) and lactate dehydrogenase (LCD-209, LCD-211), lipoprotein lipase (LPL-311, LPL-314) in clinical analysis
Physical properties
Isoelectric point : 4.2
Michaelis constants : 4.4 x 10-5M (Glycerol), 4.3 x 10-4M (ATP)
Inhibitors : p-Chloromercuribenzoate, heavy metal ions (Pb++, Fe++, Hg++, Ag+)
Optimum pH : 9.8 (G-3-PDH system), 7.8 (G-3-P oxidase system) Optimum temperature : 500C
pH Stability : pH 5.5 x 10.0 (25oC, 20hr)
Thermal stability : below 40oC (pH 7.5, 15min)
Substrate specificity : This enzyme catalyzes the stereospecific transfer of the terminal
phosphoryl moiety of ATP to one of the primary hydroxyl group of
glycerol, forming sn-glycerol-3-P. The enzyme has the highest
specificity for glycerol, and also phosphorylates dihydroxyacetone
and glyceraldehyde (Table 1,2). Mg++ is essentially required for the
reaction.
Michaelis constants : 4.4 x 10-5M (Glycerol), 4.3 x 10-4M (ATP)
Inhibitors : p-Chloromercuribenzoate, heavy metal ions (Pb++, Fe++, Hg++, Ag+)
Optimum pH : 9.8 (G-3-PDH system), 7.8 (G-3-P oxidase system) Optimum temperature : 500C
pH Stability : pH 5.5 x 10.0 (25oC, 20hr)
Thermal stability : below 40oC (pH 7.5, 15min)
Substrate specificity : This enzyme catalyzes the stereospecific transfer of the terminal
phosphoryl moiety of ATP to one of the primary hydroxyl group of
glycerol, forming sn-glycerol-3-P. The enzyme has the highest
specificity for glycerol, and also phosphorylates dihydroxyacetone
and glyceraldehyde (Table 1,2). Mg++ is essentially required for the
reaction.
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
Lyophilized powder containing phosphate buffer salts and sodium gluconate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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S I Hayashi et al.
The Journal of biological chemistry, 242(5), 1030-1035 (1967-03-10)
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