Literature summary extracted from
Bakszt, R.; Wernimont, A.; Allali-Hassani, A.; Mok, M.W.; Hills, T.; Hui, R.; Pizarro, J.C.
The crystal structure of Toxoplasma gondii pyruvate kinase 1 (2010), PLoS ONE, 5, e12736.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.7.1.40 |
D-fructose 1,6-bisphosphate |
increases the affinity and reduces the cooperativity of substrate binding, increases Vmax by 20% |
Toxoplasma gondii |
|
2.7.1.40 |
D-fructose 2,6-bisphosphate |
- |
Toxoplasma gondii |
|
2.7.1.40 |
D-glucose 6-phosphate |
classic allosteric activation with a 6fold reduction in the apparent Km and no effect on the Vmax |
Toxoplasma gondii |
|
2.7.1.40 |
additional information |
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate |
Toxoplasma gondii |
|
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.1.40 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.1.40 |
D-Fructose 1-phosphate |
allosteric inhibitor with a 40% reduction in the Vmax |
Toxoplasma gondii |
|
2.7.1.40 |
D-glucose 1-phosphate |
allosteric inhibitor with a 40% reduction in the Vmax |
Toxoplasma gondii |
|
2.7.1.40 |
additional information |
no significant effect by D-fructose 6-phosphate and D-ribulose 1,5-bisphosphate |
Toxoplasma gondii |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.1.40 |
ATP + pyruvate |
Toxoplasma gondii |
- |
ADP + phosphoenolpyruvate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.1.40 |
Toxoplasma gondii |
Q969A2 |
- |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.7.1.40 |
ATP + pyruvate = ADP + phosphoenolpyruvate |
modeling of the catalytic mechanism, overview |
Toxoplasma gondii |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.1.40 |
ATP + pyruvate |
- |
Toxoplasma gondii |
ADP + phosphoenolpyruvate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.1.40 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.1.40 |
PK1 |
- |
Toxoplasma gondii |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.1.40 |
ATP |
- |
Toxoplasma gondii |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.1.40 |
metabolism |
pyruvate kinase catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, it is a central metabolic regulator |
Toxoplasma gondii |
2.7.1.40 |
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 |