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Literature summary extracted from

  • Kobayashi, H.; Ozawa, K.; Yamada, S.
    Physical and catalytic properties of pyruvate kinase from pig dental pulp (1986), Arch. Oral Biol., 31, 559-563.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.40 D-fructose 1,6-diphosphate activation Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.40 additional information no substrate inhibition at pH-optimum Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.40 additional information
-
 additional information kinetic study Sus scrofa
2.7.1.40 0.04 0.063 phosphoenolpyruvate
-
 Sus scrofa
2.7.1.40 0.2 0.35 ADP
-
 Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.40 63000
-
 4 * 63000, SDS-PAGE Sus scrofa
2.7.1.40 250000
-
 gel filtration Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.40 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.40
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.40 dental pulp
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.40 ADP + phosphoenolpyruvate
-
 Sus scrofa ATP + pyruvate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.40 tetramer 4 * 63000, SDS-PAGE Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.40 7.2
-
-
 Sus scrofa

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.40 Sus scrofa
-
-
 8