2.7.1.146: ADP-specific phosphofructokinase
This is an abbreviated version!
For detailed information about ADP-specific phosphofructokinase, go to the full flat file.
Word Map on EC 2.7.1.146
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2.7.1.146
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hyperthermophilic
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embden-meyerhof
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archaeon
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methanococcus
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jannaschii
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amp
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furiosus
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thermococcus
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atp-pfks
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phosphofructokinases
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ppi-dependent
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fructose-1,6-bisphosphate
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sulfate-reducing
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archaeoglobus
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fulgidus
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pyrophosphate-dependent
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zilligii
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thermococcales
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eucarya
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horikoshii
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adp-forming
- 2.7.1.146
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hyperthermophilic
-
embden-meyerhof
- archaeon
-
methanococcus
- jannaschii
- amp
- furiosus
- thermococcus
- atp-pfks
-
phosphofructokinases
-
ppi-dependent
- fructose-1,6-bisphosphate
-
sulfate-reducing
-
archaeoglobus
- fulgidus
-
pyrophosphate-dependent
- zilligii
- thermococcales
- eucarya
- horikoshii
-
adp-forming
Reaction
Synonyms
ADP dependent phosphofructokinase, ADP-6-phosphofructokinase, ADP-dependent 6-phosphofructokinase, ADP-dependent glucokinase, ADP-dependent glucokinase/phosphofructokinase, ADP-dependent PFK, ADP-dependent phosphofructokinase, ADP-GK, ADP-Pfk, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, MevePFK/GK, MJ1604, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, PFK, PFK-ADP, pfkC, PhPFK, TK0376, TLPFK
ECTree
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Crystallization
Crystallization on EC 2.7.1.146 - ADP-specific phosphofructokinase
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molecular modeling of structure. for binding of ADP, residues M347, I431 and L441 create a hydrophobic pocket around the adenine group. R194 makes a hydrogen bond with alpha and beta phosphates, carbonyl and NH groups from V432 peptide bond make a hydrogen bond with the NH2 group of C6 and the N1 atom of adenine
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
hanging drop vapor diffusion method, the apo-enzyme is crystallized using 22% PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M LiSO4, at 21°C. Crystals of the PFK complex with AMP are obtained by crystallization of the PFK D17A protein in the presence of 20% PEG 3350, 0.2 M lithium citrate, 10 mM D-fructose 6-phosphate, and 5 mM ADP
through hanging drop vapor diffusion at 21°C by mixing protein solution with solution consisting of 22% PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M Li2SO4, crystals of the ADP-dependent 6-phosphofructokinase complex with AMP are obtained by crystallization of the mutant protein D17A protein in the presence of 20% PEG 3350, 0.2 M lithium citrate, 10 mM fructose 6-phosphate, and 5 mM ADPcrystal structure of ADP-dependent 6-phosphofructokinase in both apo- and AMP-bound forms determined to 2.0 A and 1.9 A resolution
purified recombinant enzyme, sitting drop vapour diffusion method, 0.005 ml of 10 mg/ml protein in 150 mM NaCl, 5 mM Tris-HCl, pH 7.5, is mixed with an equal volume of reservoir solution containing 4 M NaCl, 100 mM Tris-HCl, pH 7.5, 1 week at 25°C, derivatization by soaking for 2 days in 2.85 mM K2PtCl4, 2.8 mM HAuCl4, and 2 mM 4-hydroxymercuribenzoic acid or 0.4 mM 4-hydroxymercuribenzenesulfonic acid, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified enzyme mutant E72A, hanging drop vapor diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 25 mM HEPES/NaOH, pH 7.8, 30 mM MgCl2, 20 mM fructose 6-phosphate, and 20 mM AMP with 0.002 ml of reservoir solution containing 18% PEG 3350 and 0.15 M NaI, 3 days at 18°C, X-ray diffraction structure determination and analysis at 2.61 A resolution, molecular replacement using the structure of Pyrococcus horikoshii ADP-PFK (PDB ID 3DRW) split into small and large domains as search models
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purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 2.86 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
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purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models
purified enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein, 2.5 mM ADP, 200 mM NaCl, 7.5 mM MgCl2, 25 mM HEPES, pH 7.8, and 1 mM 2-mercaptoethanol with 0.001 ml of reservoir solution containing 20 mM CdCl2, 20 mM MgCl2, 20 mM NiCl2, 24% PEG MME 2000, and 100 mM sodium acetate, pH 4.5, 2 weeks, 19°C, X-ray diffraction structure determination and analysis at 1.46 A resolution, molecular replacement using the structure of the ancestral ADP-dependent kinase (PDB ID 5K27) split into small and large domains as search models