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Maurino, Verónica G.; Saigo, Mariana; Andreo, Carlos S.; Drincovich, Marı́a F.

doi:10.1023/a:1010665910095

Cited by 65 publications

(31 citation statements)

References 32 publications

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“…1.1.1.40) (NADP-ME) from C 3 plant Nicotiana tabacum L. was investigated. A relationship between the non-photosynthetic isoform of NADP-ME and plant defence response was suggested in our previous work and also by other authors [4–10]. NADP-ME catalyzes the oxidative decarboxylation of l -malate using NADP + as a coenzyme in the presence of divalent metal ions (Mg 2+ or Mn 2+ ions) to produce pyruvate, NADPH and CO 2 [11,12].…”

Section: Introductionmentioning

confidence: 69%

Effect of Potato Virus Y on the NADP-Malic Enzyme from Nicotiana tabacum L.: mRNA, Expressed Protein and Activity

Doubnerová

Müller

Čeřovská

et al. 2009

IJMS

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The effect of biotic stress induced by viral infection (Potato virus Y, strain NTN and O) on NADP-malic enzyme (EC 1.1.1.40) in tobacco plants (Nicotiana tabacum L., cv. Petit Havana, SR1) was tested at the transcriptional, translational and activity level. The increase of enzyme activity in infected leaves was correlated with the increased amount of expressed protein and with mRNA of cytosolic NADP-ME isoform. Transcription of the chloroplastic enzyme was not influenced by viral infection. The increase of the enzyme activity was also detected in stems and roots of infected plants. The effect of viral infection induced by Potato virus Y, NTN strain, causing more severe symptoms, was compared with the effect induced by milder strain PVYO. The observed increase in NADP-malic enzyme activity in all parts of the studied plants was higher in the case of PVYNTN strain than in the case of strain PVYO. The relevance of NADP-malic enzyme in plants under stress conditions was discussed.

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Section: Introductionmentioning

confidence: 69%

Effect of Potato Virus Y on the NADP-Malic Enzyme from Nicotiana tabacum L.: mRNA, Expressed Protein and Activity

Doubnerová

Müller

Čeřovská

et al. 2009

IJMS

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“…To rule out the possibility of a nonspecific interaction of NAD-ME2 with the affinity column, E. coli expressing only NAD-ME2 without the His tag was similarly treated (Fig. 1A, lanes [5][6][7]. In this case, NAD-ME2 mature protein was detected in bacterial extracts (Fig.…”

Section: Heterologous Co-expression Of Arabidopsis Nad-me1 and -2 Andmentioning

confidence: 99%

Three Different and Tissue-specific NAD-Malic Enzymes Generated by Alternative Subunit Association in Arabidopsis thaliana

Tronconi

Maurino

Andreo

et al. 2010

Journal of Biological Chemistry

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The Arabidopsis thaliana genome contains two genes encoding the mitochondrial NAD-malic enzyme (NAD-ME), NAD-ME1 (At2g13560) and NAD-ME2 (At4g00570). The characterization of recombinant NAD-ME1 and -2 indicated that both enzymes assemble as active homodimers; however, a heterodimeric enzyme (NAD-MEH) can also be detected by electrophoretic studies. To analyze the metabolic contribution of each enzymatic entity, NAD-MEH was obtained by a co-expression-based recombinant approach, and its kinetic and regulatory properties were analyzed. The three NAD-MEs show similar kinetic properties, although they differ in the regulation by several metabolic effectors. In this regard, whereas fumarate activates NAD-ME1 and CoA activates NAD-ME2, both compounds act synergistically on NAD-MEH activity. The characterization of two chimeric enzymes between NAD-ME1 and -2 allowed specific domains of the primary structure, which are involved in the differential allosteric regulation, to be identified. NAD-ME1 and -2 subunits showed a distinct pattern of accumulation in the separate components of the floral organ. In sepals, the NAD-ME1 subunit is present at a slightly higher proportion than the NAD-ME2 subunit, and thus, NAD-MEH and NAD-ME1 act in concert in this tissue. On the other hand, NAD-ME2 is the only isoform present in anthers. In view of the different properties of NAD-ME1, -2, and -H, we suggest that mitochondrial NAD-ME activity may be regulated by varying native association in vivo, rendering enzymatic entities with distinct allosteric regulation to fulfill specific roles. The presence of three different NAD-ME entities, which originate by alternative associations of two subunits, is suggested to be a novel phenomenon unique to plant mitochondria.

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“…Higher activity of NADP-ME caused by viral infection 9 and by abiotic stress factors in plants were found. [6][7][8][10][11][12][13][14][15][16][17] In regard to the significance of NADP-ME in plant defense response, and the quite different regulation of NADP-ME in respective organism, cells and cell compartments, it is important to bring new information into this field.…”

Section: Discussionmentioning

confidence: 99%

The regulation and catalytic mechanism of the NADP-malic enzyme from tobacco leaves

Doubnerová

Potůcková

Müller

et al. 2009

JSCS

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The non-photosynthetic NADP-malic enzyme EC 1.1.1.40 (NADP-ME), which catalyzes the oxidative decarboxylation of L-malate and NADP + to produce pyruvate and NADPH, respectively, and which could be involved in plant defense responses, was isolated from Nicotiana tabacum L. leaves. The mechanism of the enzyme reaction was studied by the initial rate method and was found to be an ordered sequential one. Regulation possibilities of purified cytosolic NADP-ME by cell metabolites were tested. Intermediates of the citric acid cycle (α-ketoglutarate, succinate, fumarate), metabolites of glycolysis (pyruvate, phosphoenolpyruvate, glucose-6-phosphate), compounds connected with lipogenesis (coenzyme A, acetyl-CoA, palmitoyl-CoA) and some amino acids (glutamate, glutamine, aspartate) did not significantly affect the NADP-ME activity from tobacco leaves. In contrast, macroergic compounds (GTP, ATP and ADP) were strong inhibitors of NADP-ME; the type of inhibition and the inhibition constants were determined in the presence of the most effective cofactors (Mn 2+ or Mg 2+ ), required by NADP-ME. Predominantly non-competitive type of inhibitions of NADP-ME with respect to NADP + and mixed type to L-malate were found.

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Cited by 65 publications

References 32 publications

Effect of Potato Virus Y on the NADP-Malic Enzyme from Nicotiana tabacum L.: mRNA, Expressed Protein and Activity

Effect of Potato Virus Y on the NADP-Malic Enzyme from Nicotiana tabacum L.: mRNA, Expressed Protein and Activity

Three Different and Tissue-specific NAD-Malic Enzymes Generated by Alternative Subunit Association in Arabidopsis thaliana

The regulation and catalytic mechanism of the NADP-malic enzyme from tobacco leaves

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