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Kinetic mechanism of NADP-malic enzyme from maize leaves

Photosynthesis Research volume 43, pages 1–9 (1995)Cite this article

Abstract

The kinetic mechanism of NADP-dependent malic enzyme purified from maize leaves was studied in the physiological direction. Product inhibition and substrate analogues studies with 3′ aminopyridine dinucleotide phosphate and tartrate indicate that the enzyme reaction follows a sequential ordered Bi-Ter kinetic mechanism. NADP is the leading substrate followed by l-malate and the products are released in the order of CO2, pyruvate and NADPH. The enzyme also catalyzes a slow, magnesium-dependent decarboxylation of oxaloacetate and reduction of pyruvate and oxaloacetate in the presence of NADPH to produce l-lactate and l-malate, respectively.

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Affiliations

  1. Centro de Estudios Fotosintéticos y Bioquímicos (CONICET, F.M. Lillo, Universidad Nacional de Rosario, Suipacha 531, 2000, Rosario, Argentina

    Claudia P. Spampinato & Carlos S. Andreo

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  1. Claudia P. Spampinato
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  2. Carlos S. Andreo
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Spampinato, C.P., Andreo, C.S. Kinetic mechanism of NADP-malic enzyme from maize leaves. Photosynth Res 43, 1–9 (1995). https://doi.org/10.1007/BF00029456

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  • DOI: https://doi.org/10.1007/BF00029456

Key words

  • Zea mays
  • C4-photosynthesis
  • decarboxylation
  • NADP-ME type
  • reaction mechanism