Literature DB >> 7067906

Isocitrate lyase of conifers (Pinus pinea).

G Pinzauti, E Giachetti, P Vanni.   

Abstract

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.

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Year:  1982        PMID: 7067906     DOI: 10.1016/0020-711x(82)90087-8

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  2 in total

1.  Differential induction of glyoxylate cycle enzymes by stress as a marker for seedling vigor in sugar beet (Beta vulgaris).

Authors:  B G de los Reyes; S J Myers; J M McGrath
Journal:  Mol Genet Genomics       Date:  2003-06-27       Impact factor: 3.291

2.  Purification and characterization of Acinetobacter calcoaceticus isocitrate lyase.

Authors:  J C Hoyt; K E Johnson; H C Reeves
Journal:  J Bacteriol       Date:  1991-11       Impact factor: 3.490

  2 in total

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