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Literature summary for 2.7.1.40 extracted from

  • Michaelidis, B.; Lazou, A.; Beis, I.
    Purification, catalytic and regulatory properties of pyruvate kinase from the foot of Patella caerulea (L.) (1985), Comp. Biochem. Physiol. B, 82, 405-412.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
D-fructose diphosphate activation Patella caerulea

Inhibitors

Inhibitors Comment Organism Structure
L-alanine fructose bisphosphate protects; strong Patella caerulea
L-phenylalanine fructose 1,6-diphosphate protects; not in the presence of Mn2+; strong Patella caerulea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic properties Patella caerulea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
238000
-
native MW Patella caerulea

Organism

Organism UniProt Comment Textmining
Patella caerulea
-
limpet
-

Purification (Commentary)

Purification (Comment) Organism
-
Patella caerulea

Source Tissue

Source Tissue Comment Organism Textmining
foot
-
Patella caerulea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Patella caerulea

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
Patella caerulea