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Inactivation of maize NADP-malic enzyme by Cu2+-ascorbate.

S E Pinto1, S R Rao, A S Bhagwat

  • 1Molecular Biology and Agriculture Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.

Indian Journal of Biochemistry & Biophysics
|August 18, 2012
PubMed
Summary
This summary is machine-generated.

Cupric nitrate and ascorbate rapidly inactivate maize malic enzyme by generating reactive oxygen species. This inactivation involves enzyme cleavage, potentially near the substrate-binding site.

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Area of Science:

  • Biochemistry
  • Plant Physiology
  • Enzymology

Background:

  • Maize malic enzyme is crucial for plant metabolism.
  • Understanding enzyme regulation and inactivation is vital for agricultural applications.

Purpose of the Study:

  • To investigate the inactivation mechanism of maize malic enzyme by the cupric ion-ascorbate system.
  • To identify the reactive species involved and the effect on enzyme structure.

Main Methods:

  • Enzyme activity assays were performed under various conditions.
  • Protective agents (L-malate, NADP, EDTA, histidine, imidazole) were used.
  • Protease inhibitors and reactive oxygen species scavengers were employed.
  • Peptide cleavage analysis using molecular mass determination.

Main Results:

  • Cupric nitrate and ascorbate rapidly inactivated maize malic enzyme at pH 5.0.
  • Inactivation was prevented by L-malate or NADP, suggesting substrate protection.
  • Enzyme cleavage into peptides (55, 48, 38, 14 kDa) occurred during inactivation.
  • Reactive oxygen species, including singlet oxygen and H2O2, were implicated.
  • Protection by EDTA, histidine, and imidazole indicated metal ion involvement.

Conclusions:

  • The cupric ion-ascorbate system generates reactive oxygen species that inactivate maize malic enzyme.
  • Inactivation involves enzyme cleavage, likely at or near the substrate-binding site.
  • Understanding this inactivation pathway is important for maize enzyme stability and function.