G0774
Glycerokinase from Bacillus stearothermophilus
buffered aqueous solution, ≥75 units/mg protein (biuret)
Synonym(s):
ATP:glycerol 3-phosphotransferase, Glycerol Kinase
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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-862-0
NACRES:
NA.54
MDL number:
Specific activity:
≥75 units/mg protein (biuret)
Assay:
≥5.0 mg protein/mL (biuret)
Biological source:
Bacillus sp. (Bacillus steaarothermophilus)
biological source
Bacillus sp. (Bacillus steaarothermophilus)
assay
≥5.0 mg protein/mL (biuret)
form
buffered aqueous solution
specific activity
≥75 units/mg protein (biuret)
storage condition
dry at room temperature
color
beige
application(s)
life science and biopharma
storage temp.
2-8°C
Quality Level
Gene Information
Bacillus sp. ... glpK(89613566)
General description
Research area: Cell Signaling
Glycerol kinase is encoded by the GK gene on chromosome Xp21.2. Glycerol kinase is predominantly active in the liver.
Glycerol kinase is encoded by the GK gene on chromosome Xp21.2. Glycerol kinase is predominantly active in the liver.
Application
Glycerokinase from Bacillus stearothermophilus has been used in steady-state kinetics studies.
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.Oxidized glycerol-3-phosphate results in dihydroxyacetone phosphate which enters either glycolysis or gluconeogenesis. Elevated glycerol is observed in glycerol kinase deficiency leading to pseudohypertriglyceridemia.
Physical form
Stabilized solution in Tris buffer, pH 7.3
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.
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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N Zwaig et al.
Science (New York, N.Y.), 153(3737), 755-757 (1966-08-12)
Fructose-1 ,6-diphosphate is a feedback inhibitor of the catabolic enzyme, glycerol kinase, in Escherichia coli. A mutant was isolated which produced a desensitized enzyme. Glucose was no longer as effective in preventing the utilization of exogenous glycerol by cells which
Purification and properties of glycerol kinase from Escherichia coli.
S I Hayashi et al.
The Journal of biological chemistry, 242(5), 1030-1035 (1967-03-10)
N Zwaig et al.
Journal of bacteriology, 102(3), 753-759 (1970-06-01)
The activity of glycerol kinase is rate-limiting in the metabolism of glycerol by cells of Escherichia coli. A mutant strain producing a glycerol kinase resistant to inhibition by fructose-1,6-diphosphate grows faster than its wild-type parent on glycerol as the sole
Carol J Hartley et al.
PloS one, 12(11), e0184183-e0184183 (2017-11-08)
Carbon-carbon bond formation is one of the most challenging reactions in synthetic organic chemistry, and aldol reactions catalysed by dihydroxyacetone phosphate-dependent aldolases provide a powerful biocatalytic tool for combining C-C bond formation with the generation of two new stereo-centres, with
M Kenyon Applebee et al.
The Journal of biological chemistry, 286(26), 23150-23159 (2011-05-10)
Herein we measure the effect of four adaptive non-synonymous mutations to the glycerol kinase (glpK) gene on catalytic function and regulation, to identify changes that correlate to increased fitness in glycerol media. The mutations significantly reduce affinity for the allosteric
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