Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-fructose 1,6-bisphosphate | increases the affinity and reduces the cooperativity of substrate binding, increases Vmax by 20% | Toxoplasma gondii | |
D-fructose 2,6-bisphosphate | - |
Toxoplasma gondii | |
D-glucose 6-phosphate | classic allosteric activation with a 6fold reduction in the apparent Km and no effect on the Vmax | Toxoplasma gondii | |
additional information | no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate | Toxoplasma gondii |
Crystallization (Comment) | Organism |
---|---|
purified recombinant N-terminally His6-tagged full-length and N-terminaly truncated enzymes, with the B domain in the open and closed conformations, crystals of the truncated TgPK1 are grown in the presence of K+, Mg2+, and inhibitor, X-ray diffraction structure determination and analysis | Toxoplasma gondii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-Fructose 1-phosphate | allosteric inhibitor with a 40% reduction in the Vmax | Toxoplasma gondii | |
D-glucose 1-phosphate | allosteric inhibitor with a 40% reduction in the Vmax | Toxoplasma gondii | |
additional information | no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate | Toxoplasma gondii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate | Toxoplasma gondii | - |
ADP + phosphoenolpyruvate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Toxoplasma gondii | Q969A2 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + pyruvate = ADP + phosphoenolpyruvate | modeling of the catalytic mechanism, overview | Toxoplasma gondii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate | - |
Toxoplasma gondii | ADP + phosphoenolpyruvate | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | each monomer is composed of four domains: A, B, C and N, structure, overview. The central A domain, residues I59-G124 and V224-C393, is composed of an (alpha/beta)8 barrel. The B-domain, P125-P223, is composed of only beta-strands and random coils. The catalytic site is located at the interface of these two domains, where residues in domain A interact with PEP and ADP and residues from the B domain contact ADP and Mg2+. The C domain, residues V394-E531, is composed of alpha and beta structural elements. It contains the effector binding/allosteric site. The N-terminal domain includes the first fifty amino acids of the protein and is a helix-loop-helix motif, however in the TgPK1 only a single helix is observed | Toxoplasma gondii |
Synonyms | Comment | Organism |
---|---|---|
PK1 | - |
Toxoplasma gondii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Toxoplasma gondii |
General Information | Comment | Organism |
---|---|---|
metabolism | pyruvate kinase catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, it is a central metabolic regulator | Toxoplasma gondii |
additional information | allosteric site structure and regulation, overview. Comparison of the B domain open and closed conformation shows reorientation of the monomers with a concomitant change in the buried surface among adjacent monomers. The change in the buried surface is associated with significant B domain movements in one of the interacting monomers. A loop in the interface between the A and B domains plays an important role linking the position of the B domain to the buried surface among monomers through two alpha-helices. An unusual ordered conformation is observed in one of the allosteric binding domains, it is related to a specific apicomplexan insertion | Toxoplasma gondii |