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G0774

Sigma-Aldrich

Glycerokinase from Bacillus stearothermophilus

buffered aqueous solution, ≥75 units/mg protein (biuret)

Sinónimos:

ATP:glycerol 3-phosphotransferase, Glycerol Kinase

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About This Item

Número de CAS:
9030-66-4
Comisión internacional de enzimas:
2.7.1.30 (BRENDA, IUBMB)
EC Number:
232-862-0
MDL number:
MFCD00131205
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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

Gene Information

Bacillus sp. ... glpK(89613566)

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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.

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.

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

Stabilized solution in Tris buffer, pH 7.3

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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
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.
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
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
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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