Literature summary for 2.7.1.40 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.

Search for more literature for 2.7.1.40

Activating Compound

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 (Commentary)

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

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + pyruvate	Toxoplasma gondii	-	ADP + phosphoenolpyruvate	-	?

Organism

Organism	UniProt	Comment	Textmining
Toxoplasma gondii	Q969A2	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + pyruvate = ADP + phosphoenolpyruvate	modeling of the catalytic mechanism, overview	Toxoplasma gondii	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + pyruvate	-	Toxoplasma gondii	ADP + phosphoenolpyruvate	-	?

Subunits

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

Synonyms	Comment	Organism
PK1	-	Toxoplasma gondii

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Toxoplasma gondii

General Information

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

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Release 2023.1 (January 2023)