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Literature summary for 2.7.1.40 extracted from

  • Ou, Y.; Tao, W.; Zhang, Y.; Wu, G.; Yu, S.
    The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates (2010), Int. J. Biol. Macromol., 47, 228-232.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-phenylalanine acts as an allosteric inhibitor of muscle isozyme and induces the enzyme to exist in multiple conformations by locking it in an expanded or asymmetric conformation, which is contrary effect to that of phosphoenolpyruvate binding Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required Oryctolagus cuniculus
Mg2+ required Oryctolagus cuniculus
additional information enzyme spectra in the absence and presence of activating cations, overview 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
-
r

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
-
r

Subunits

Subunits Comment Organism
homotetramer secondary and tertiary structure of muscle isozyme homotetramer and the four monomers with three tryptophans Trp157, Trp481, and Trp514, and bound Mg2+ and K+ per monomer, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
aassay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ADP
-
Oryctolagus cuniculus
ATP
-
Oryctolagus cuniculus

General Information

General Information Comment Organism
additional information catalysis by muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg2+ and K+ lead to a more exposed active site of the enzyme while interactions with phosphoenolpyruvate and ADP decrease solvent accessibility of the active site, overview Oryctolagus cuniculus