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isocitrate lyase/tusam
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[Lactate as competitive inhibitor of Pinus pinea isocitrate lyase].
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We studied the effect of L-lactate on both the cleavage and the condensation reactions of Pinus pinea isocitrate lyase. This compound is a competitive of Pinus pinea isocitrate lyase towards both isocitrate and glyoxylate, whereas is a mixed type inhibitor towards succinate. Assuming that L-lactate
On the stability of isocitrate lyase from Pinus pinea.
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Isocitrate lyase is a key catalyst of the glyoxylate cycle. A feature of the enzyme from higher plants is the high instability, that causes innumerable problems in working for characterization of the enzyme. The present communication demonstrates that the optimal conditions for the storage of
Multisite inhibition of Pinus pinea isocitrate lyase by phosphate.
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Our results show that the phosphate ion is a nonlinear competitive inhibitor of Pinus pinea isocitrate lyase. In addition, this compound induces a sigmoidal response of the enzyme, which usually exhibits standard Michaelis-Menten kinetics. This peculiar behavior of P. pinea isocitrate lyase could be
The Effects of Octanoate and Oleate on Isocitrate Lyase Activity during the Germination of Pinus pinea Seeds.
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The changes of isocitrate lyase levels with respect to the catabolism of triglycerides have been studied during the germination of Pinus pinea seeds. We studied the effects of octanoate, oleate, and inhibitors of protein synthesis on isocitrate lyase during germination. Pyruvate kinase,
Isocitrate lyase activities in Pinus pinea seeds.
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Some features of cytoplasmic and glyoxysomal isocitrate lyase obtained from stratified and germinated P. pinea seeds, respectively, are described. Both activities showed a different electrophoretic mobility on cellulose acetate and elution behaviour on Sephadex G-200. Cycloheximide inhibited the
Isocitrate lyase: artifacts and multiple enzyme forms.
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Multiple enzyme forms of isocitrate lyase from various sources have been frequently reported. Protease action after cell rupture was sporadically claimed to explain the observed multiple enzyme forms. In this communication studies which are consistent with a protease action in vitro on isocitrate
An isocitrate lyase of higher plants: analysis and comparison of some molecular properties.
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A new purification procedure for isocitrate lyase from Pinus pinea is reported. The final preparation shows charge homogeneity and a purity degree higher than 95%. It is possible to remove catalase completely by exploiting the high hydrophobicity of isocitrate lyase. The enzyme has a Mr of 264,000
Isocitrate lyase from Pinus pinea. Characterization of its true substrate and the action of magnesium ions.
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We found that the Mg-isocitrate complex is the true substrate for pine isocitrate lyase and that magnesium acts as a non-essential activator. Both the non-activated and the activated enzyme forms are catalytically active. Our model is consistent with the presence of two Mg-binding sites with
Biochemical changes in Pinus pinea seeds. II. The stimulation is isocitrate lyase and malate dehydrogenase activities by exogenous growth substances.
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Treatment of intact pine seeds with plant hormones and steroid substances for several days, after an initial 24 hour immersion in different hormone solutions, resulted in a substantial increase in the specific activity of isocitrate lyase and malate dehydrogenase than the observed in the
Regulation of two loblolly pine (Pinus taeda L.) isocitrate lyase genes in megagametophytes of mature and stratified seeds and during postgerminative growth.
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Two full-length cDNAs encoding the glyoxysomal enzyme isocitrate lyase (ICL) were isolated from a lambda ZAP cDNA library prepared from megagametophyte mRNAs extracted from seeds imbibed at 30 degrees C for 8 days. The cDNAs, designated Ptbs ICL 8 and Ptbs ICL 12, have open reading frames of 1740
Isocitrate lyase of conifers (Pinus pinea).
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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
Purification and some properties of isocitrate lyase from Pinus pinea.
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On the possible intracellular localization of isocitrate lyase from Pinus pinea.
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Gravitational stress on germinating Pinus pinea seeds.
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In the germination of lipid-rich seeds, the glyoxylate cycle plays a control role in that, bypassing the two decarboxylative steps of the Krebs cycle; it allows the net synthesis of carbohydrates from lipids. The activity of isocitrate lyase, the key enzyme of the glyoxylate cycle, is an indicator
Glyoxylate cycle activity in Pinus pinea seeds during germination in altered gravity conditions.
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This work inserts in the research field regarding the effects of altered gravity conditions on biological plant processes. Pinus pinea seeds germination was studied in simulated microgravity (2x10-3g) and hypergravity (20g) conditions. The effects of simulated gravity were evaluated
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