Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
oligomeric state observed in the crystal is tetrameric, structural elements involved in the binding of the substrate and allosteric ATPs are also participating in the dimer-dimer interface, data collection parameters and structure refinement statistics | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
MgATP | inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for activity, MgATP is the active substrate | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
66000 | - |
native protein, SDS-PAGE | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
monomer structure and structural features of intersubunit interactions, interactions with ligands at the active site, structure determination in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions, allosteric site reported for ATP, analogous structural features in the 6-phosphofructokinases from Escherichia coli compared | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | mechanism of enzyme inhibition by ATP analyzed by structure determination | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer, oligomerization state necessary for catalysis and stability, presence of MgATP favors the tetrameric form of the enzyme | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
Pfk-2 | - |
Escherichia coli |