منابع مشابه
Isocitrate lyase from Phycomyces blakesleeanus
Isocitrate lyase was purified from Phycomyces blakesleeanus N.R.R.L. 1555(-). The native enzyme has an Mr of 240000. The enzyme appeared to be a tetramer with apparently identical subunits of Mr 62000. The enzyme requires Mg2+ for activity, and the data suggest that the Mg2+-isocitrate complex is the true substrate and that Mg2+ ions act as a nonessential activator. The kinetic mechanism of the...
متن کاملSynthesis of Glycolate from Pyruvate via Isocitrate Lyase by Tobacco Leaves in Light.
Tobacco (Nicotiana tabacum var Havana Seed) leaf discs were supplied tracer quantities of [2-(14)C]- and [3-(14)C]pyruvate for 60 minutes in steady state photosynthesis with 21% or 1% O(2), and the glycolate oxidase inhibitor alpha-hydroxy-2-pyridinemethanesulfonic acid was then added for 5 or 10 minutes to cause glycolate to accumulate. The [3-(14)C]pyruvate was converted directly to glycolate...
متن کاملStereochemical Course of the Isocitrate Lyase Reaction.
The formation of glyoxylate and succinate from citrate or cis-aconitate, and the reverse reaction, were first observed by Campbell, Smith, and Eagles (1) in extracts of Pseudomonas aeruginosa. Later, it was established by Smith and Gunsalus (2) and other investigators (3-5) that three-n,-isocitrate is the actual substrate, and that the enzyme, isocitrate lyase, is characteristically induced in ...
متن کاملEffect of glucose on isocitrate lyase in Phycomyces blakesleeanus.
Repression of the synthesis of isocitrate lyase by glucose and/or induction of the synthesis of isocitrate lyase by acetate in Phycomyces blakesleeanus were demonstrated. Both glycerol and ethanol failed to induce isocitrate lyase activity. Furthermore, glucose appeared to cause an in vivo catabolite inactivation of the derepressed enzyme. Isocitrate lyase was inactivated both reversibly and ir...
متن کاملRole of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli.
Phosphoenolpyruvate inhibited Escherichia coli NADP-isocitrate dehydrogenase allosterically (Ki of 0.31 mM) and isocitrate lyase uncompetitively (Ki' of 0.893 mM). Phosphoenolpyruvate enhances the uncompetitive inhibition of isocitrate lyase by increasing isocitrate, which protects isocitrate dehydrogenase from the inhibition, and contributes to the control through the tricarboxylic acid cycle ...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1973
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.51.5.863