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Literature summary for 4.1.3.1 extracted from

  • Ranaldi, F.; Vanni, P.; Giachetti, E.
    Enzyme catalysis in microgravity: steady-state kinetic analysis of the isocitrate lyase reaction (2003), Biophys. Chem., 103, 169-177.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.039
-
isocitrate pH 7, standard g, cleavage reaction Pinus pinea
0.043
-
isocitrate pH 7, microgravity, cleavage reaction Pinus pinea
0.053
-
succinate pH 7, microgravity, condensation reaction Pinus pinea
0.063
-
succinate pH 7, standard g, condensation reaction Pinus pinea
0.088
-
glyoxylate pH 7, microgravity, condensation reaction Pinus pinea
0.092
-
glyoxylate pH 7, standard g, condensation reaction Pinus pinea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
isocitrate Pinus pinea
-
succinate + glyoxylate
-
r

Organism

Organism UniProt Comment Textmining
Pinus pinea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pinus pinea

Reaction

Reaction Comment Organism Reaction ID
isocitrate = succinate + glyoxylate kinetic mechanism is the same in microgravity and in standard g controls Pinus pinea

Source Tissue

Source Tissue Comment Organism Textmining
seed germinating Pinus pinea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate
-
Pinus pinea succinate + glyoxylate
-
r