Isocitrate lyase of conifers (Pinus pinea).
1. Isocitrate lyase has been purified about 60 times from the conifer Pinus pinea. A first characterization was made. 2. The high instability is an important feature of this enzyme from higher plants, this causes serious problems in the purification and characterization. 3. A substantial agreement with the data from the literature was found for what concerns pH dependence of Vmax and pKm, the effect of bivalent cations and the requirement of Mg2+. 4. Kinetic studies gave evidence for a mechanism ordered uni-bi with glyoxylate being the last product released, kinetic constants were calculated, no evidence for cooperative effects was found. 5. Equilibrium constant by Haldane method calculation agrees with value calculated with isocitrate lyase from the bacterium Pseudomonas indigofera.
D002413:Cations, Divalent / Q000494:pharmacology; D006038:Glyoxylates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007522:Isocitrate Lyase / Q000302:isolation & purification*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D007652:Oxo-Acid-Lyases / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology*; D013386:Succinates / Q000378:metabolism; D019802:Succinic Acid; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013997:Time Factors
D002413:Cations, Divalent; D006038:Glyoxylates; D013386:Succinates; D013438:Sulfhydryl Compounds; D019802:Succinic Acid; D007652:Oxo-Acid-Lyases; D007522:Isocitrate Lyase; D008274:Magnesium; C031150:glyoxylic acid