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Literature summary for 2.7.1.40 extracted from

  • Urness, J.M.; Clapp, K.M.; Timmons, J.C.; Bai, X.; Chandrasoma, N.; Buszek, K.R.; Fenton, A.W.
    Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase (2013), Biochemistry, 52, 1-3.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.40

Inhibitors

Inhibitors Comment Organism Structure
L-phenylalanine the carboxyl group of phosphoenolpyruvate is responsible for energetic coupling with Phe binding in the allosteric sites Oryctolagus cuniculus
additional information replacing the carboxyl group of the substrate with a methyl alcohol or removing the phosphate altogether greatly reduces substrate affinity. Removal of the carboxyl group is the only modification tested that removes the ability to allosterically reduce the level of Phe binding. Requirement for monovalent and divalent cations for allosteric inhibition Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
M1-PYK
-
 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
physiological function required role of the active site in allosteric regulation involving substrate binding, requirement for monovalent and divalent cations, overview Oryctolagus cuniculus