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.

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

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.1 Phosphotransferases with an alcohol group as acceptor

                2.7.1.146 ADP-specific phosphofructokinase

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Results	in table
6	Activating Compound
254	AA Sequence
1	CAS Registry Number
22	Cloned(Commentary)
18	Cofactor
8	Crystallization (Commentary)
54	General Information
2	General Stability
5	IC50 Value
39	Inhibitors
71	kcat/KM [mM/s]
10	Ki Value [mM]
110	KM Value [mM]
1	Localization
83	Metals/Ions
21	Molecular Weight [Da]
53	Natural Substrates/ Products (Substrates)
78	Organism
10	Pathway
7	PDB ID
19	pH Optimum
6	pH Range
1	pI Value
35	Protein Variants
18	Purification (Commentary)
1	Reaction
2	Reaction Type
55	Reference
2	Source Tissue
22	Specific Activity [micromol/min/mg]
1	Storage Stability
130	Substrates and Products (Substrate)
16	Subunits
104	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
3	Temperature Range [°C]
8	Temperature Stability [°C]
70	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.1.146 - ADP-specific phosphofructokinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Methanococcus maripaludis

Q6LXQ3

727486

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

2 entries

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

Pyrococcus horikoshii

O59355

698924

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

Pyrococcus horikoshii

O59355

698924

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

Thermococcus litoralis

Q977Q3

660573

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

uncultured bacterium

-

761465

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

uncultured bacterium

-

761158

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

Methanohalobium evestigatum

D7E8P3

761158

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

Methanosarcina mazei

Q8PZL9

761158