2.7.1.147: ADP-specific glucose/glucosamine kinase
This is an abbreviated version!
For detailed information about ADP-specific glucose/glucosamine kinase, go to the full flat file.
Word Map on EC 2.7.1.147
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2.7.1.147
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hyperthermophilic
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thermococcus
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embden-meyerhof
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litoralis
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phosphofructokinases
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jannaschii
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furiosus
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glucokinases
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ribokinase
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methanococcales
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thermococcales
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6-phosphofructokinase
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hexokinases
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atp-pfks
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methanosarcinales
- 2.7.1.147
-
hyperthermophilic
- thermococcus
-
embden-meyerhof
- litoralis
-
phosphofructokinases
- jannaschii
- furiosus
- glucokinases
- ribokinase
- methanococcales
- thermococcales
- 6-phosphofructokinase
- hexokinases
- atp-pfks
- methanosarcinales
Reaction
Synonyms
ADP-dependent glucokinase, ADP-dependent hexokinase, ADP-dependent kinase, ADP-GK, ADP-HK, ADP-Pfk, ADP-specific glucokinase, ADP:D-glucose 6-phosphotransferase, ADPGK, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, GlcN kinase, glucosamine kinase, MevePFK/GK, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, NagC4, pfGK, pfkC, PhPFK, TK1110, tlGK
ECTree
2.7.1.147 ADP-specific glucose/glucosamine kinaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 20°C, complex of the enzyme with glucose and 8-bromoadenosine phosphate
structures reveal a ribokinase-like tertiary fold similar to archaeal orthologues but with significant differences in some secondary structural elements. Both the unliganded and the AMP-bound ADPGK structures are in the open conformation and reveal the presence of a disulfide bond between conserved cysteines that is positioned at the nucleotide-binding loop. The AMP-bound structure defines the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its main chain atoms
sitting drop vapor diffusion method at 20°C, crystal structure of the ADP-dependent glucokinase from Methanocaldococcus jannaschii in complex with the inhibitor 5-iodotubercidin
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
enzyme in complex with AMP, sitting drop vapour diffusion method, 10 mg/ml protein in 6 mM ADP-beta-S, 30 mM glucose mixed in equal volumes with reservoir solution containing 1.6 M citrate, pH 6.5, 10 mM DTT, equilibration against 0.075 ml of reservoir solution at 25°C, a few weeks to 1 month, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement, modeling
purified recombinant N-terminally His-tagged apoenzyme, hanging drop vapour diffusion method, 20°C, 10 mg/ml protein in solution is mixed with an equal volume of 0.003 ml of mother liquor containing 9-13% PEG 6000, 0.2 M Li2SO4, and 0.1 M citrate buffer, pH 3.6, heavy atom derivatization with HgCl2, X-ray diffraction structure determination and analysis at 2.0 A resolution, single isomorphous replacement with an anomalous scattering
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sitting drop vapor diffusion method at 20°C, complex of the enzyme with glucose and 8-bromoadenosine phosphate
crystal structures of apo form and holo form, in the presence of D-glucose and the nonhydrolyzable ADP analog adenosine 5'-(3-thio)diphosphate. The conformational changes upon sequential substrate binding can be explained by an almost pure rotation (or a rotation plus a translation) facilitated by residues in the flexible inter-domain connection
crystallized with ADP and Mg2+, the structure is determined by multiple isomorphous replacement with anomalous scattering and refined at 2.3 A. Crystals are grown at 25°C by the hanging drop vapor diffusion method
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
