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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.
    View publication on PubMedView publication on EuropePMC

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