2.7.1.30: glycerol kinase
This is an abbreviated version!
For detailed information about glycerol kinase, go to the full flat file.
Word Map on EC 2.7.1.30
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2.7.1.30
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glycerol-3-phosphate
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triglyceride
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adrenal
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hypoplasia
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dystrophy
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muscular
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adipose
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3-phosphate
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duchenne
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lipase
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phosphoenolpyruvate
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hexokinase
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x-linked
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dihydroxyacetone
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contiguous
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adipocytes
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triacylglycerols
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carboxykinase
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congenita
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gluconeogenesis
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glycerophosphate
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lipolysis
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hpr
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iiaglc
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1,6-bisphosphate
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hypogonadism
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co-immobilized
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phosphocarrier
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glyceroneogenesis
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hypogonadotropic
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glycosomes
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dissimilation
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triolein
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1,3-propanediol
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glucose-specific
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aquaglyceroporins
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d-glyceraldehyde
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phosphoenolpyruvate:sugar
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dhap
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phosphoenolpyruvate-dependent
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sn-glycerol-3-phosphate
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sn-glycerol
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drug development
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diagnostics
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synthesis
- 2.7.1.30
- glycerol-3-phosphate
- triglyceride
- adrenal
- hypoplasia
- dystrophy
- muscular
- adipose
- 3-phosphate
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duchenne
- lipase
- phosphoenolpyruvate
- hexokinase
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x-linked
- dihydroxyacetone
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contiguous
- adipocytes
- triacylglycerols
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carboxykinase
- congenita
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gluconeogenesis
- glycerophosphate
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lipolysis
- hpr
- iiaglc
- 1,6-bisphosphate
- hypogonadism
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co-immobilized
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phosphocarrier
-
glyceroneogenesis
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hypogonadotropic
- glycosomes
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dissimilation
- triolein
- 1,3-propanediol
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glucose-specific
-
aquaglyceroporins
- d-glyceraldehyde
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phosphoenolpyruvate:sugar
- dhap
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phosphoenolpyruvate-dependent
- sn-glycerol-3-phosphate
- sn-glycerol
- drug development
- diagnostics
- synthesis
Reaction
Synonyms
AFUB_068560, ASTP
ECTree
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Crystallization
Crystallization on EC 2.7.1.30 - glycerol kinase
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crystals are obtained by the hanging-drop technique from a solution containing 29% polyethylene glycol 400, 0.1 M sodium acetate pH 4.5, 0.1 M calcium acetate and 10% glycerol. The crystals can grow in the presence of 33% PEG 400, which allows to mount the crystals and directyl flash-cool them. Repeated flash-annealing causes a significant decrease in the averaged mosaicity along with an increase in the overall peak counts of reflections and an enhanced signal-to-noise ratio. Individual reflection-profile analysis reveales a mostly dual domain structure, showing the minimization of one domain as a result of flash-annealing.
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crystals of native and mutant enzyme with bound glycerol, hanging drop vapor diffusion method
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in complex with glycerol, in presence and absence of fructose 1,6-diphosphate, mechanism
of wild type and mutant A65T, both in complex with glycerol and ADP, and of mutant I474D, in complex with IIAGlc
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the crystal structure of glycerol kinase mutant G230D is determined to 2.0 A resolution using a microfluidics based crystallization platform
using modified microfluidic scale-up diffraction device, crystals form after one week at ambient temperature unter crystallization conditions 0.3 M magnesium chloride, 0.1 M TrisHCl (pH 8.5), and 20% PEG 1500. Using vapor diffusion crystallization, crystals appear after one week at ambient temperature using the crystallization conditions 0.1 M magnesium chloride, 0.1 M TrisHCl (pH 8.5), and 10% PEG 1500. Glycerol kinase of the mutant G230D crystallied in space group P21 with two tetramers of 222 point symmetry in the asu. The average B factor for the overall structure of the G230D mutant is 21.2 A2.
crystals are grown at 20°C by the sitting-drop vapour diffusion method. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. The protein is also cocrystallized with substrates and diffraction data are collected to 2.7 A resolution
purified recombinant wild-type enzyme in complex with glycerol and AMPPCP, and enzyme mutant K271E free or in complex with glycerol, sitting drop vapor diffusion method, 4-5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, with or without 5 mM glycerol, and 5 mM AMPPCP, is mixed with 0.1 M HEPES, pH 8.0, containing 15% w/v PEG 1000 and 200 mM calcium acetate, 20°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A resolution, molecular replacement using the structure of Tk-GK (PDB ID 2ZF5) as template, modelling
using sitting-drop vapour-diffusion method at 293 K. Native Tk-glycerol kinase crystals appear after a few days using Wizard I solution No. 25 (0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG 400). Diffraction spots sufficient for structural determination at high resolution are not obtained when a crystal of Tk-glycerol kinase is mounted on a CryoLoop without cryoprotectant, diffraction patterns of the crystal are improved by using Paratone-N as cryoprotectant. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. Assuming the presence of two molecules in the asymmetric unit, the VM value is 2.7 A3Da-1 and the solvent content is 54.1%.
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in complex with substrates, sitting drop vapor diffusion method, using M HEPES pH 7.5, 11% (v/v) hexane-1,6-diol, 25% (w/v) PEG400
purified recombinant His6-tagged enzyme in complex with pNPP, sitting drop method, mixing of 0.001 ml of 5 mg/mL TbgGK in 10 mM MgSO4, 20 mM NaCl, 0.001% glycerol and 10 mM MOPS, pH 6.8, with 0.001 ml of 11% 1,6-hexanediol, 25% PEG 400, and 0.1 M HEPES, pH 7.5, at 20°C, crystals of the TbgGK-pNPP complex are obtained by soaking TbgGK crystals in a cryoprotectant solution containing 5.5% 1,6-hexanediol, 40% PEG 400, and 0.1 M HEPES, pH 7.5, that is supplemented with 20 mM pNPP, at 20°C, for 6-14 h, X-ray diffraction structure determination and analysis, molecular replacement method using the protein structure of the TbgGK-ADP complex (PDB ID 3WXL) as a search model
sitting drop vapor diffusion method, using 30% (w/v) PEG 400 and 100 mM HEPES pH 7.0, at 20°C
purified recombinant His6-tagged enzyme in complex with pNPP, sitting drop method, mixing of 0.001 ml of 5 mg/mL TbgGK in 10 mM MgSO4, 20 mM NaCl, 0.001% glycerol and 10 mM MOPS, pH 6.8, with 0.001 ml of 11% 1,6-hexanediol, 25% PEG 400, and 0.1 M HEPES, pH 7.5, at 20°C, crystals of the TbgGK-pNPP complex are obtained by soaking TbgGK crystals in a cryoprotectant solution containing 5.5% 1,6-hexanediol, 40% PEG 400, and 0.1 M HEPES, pH 7.5, that is supplemented with 20 mM pNPP, at 20°C, for 6-14 h, X-ray diffraction structure determination and analysis, molecular replacement method using the protein structure of the TbgGK-ADP complex (PDB ID 3WXL) as a search model