The distribution and properties of NADP malic enzyme in flowering plants

Davies, Daniel; Nascimento, KS; Patil, K. D.

doi:10.1016/s0031-9422(00)86916-2

Cited by 33 publications

(8 citation statements)

References 10 publications

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“…Nevertheless, the malic enzyme found in a number of species belonging to the Graminae does not exhibit these allosteric properties. Furthermore, succinate acts as an inhibitor at high malate concentration (Davies et al 1974). In our studies, succinate did not show a significant effect either at low or high malate concentrations (0.01-0.5 raM) at both pH values.…”

Section: Resultscontrasting

confidence: 62%

Interaction of analogues of substrate with NADP-malic enzyme from maize leaves

1994

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The effect of structural analogues of L-malate was studied on NADP-malic enzyme purified from Zea mays L. leaves. Among the compounds tested, the organic acids behaved as more potent inhibitors at pH 7.0 than at pH 8.0, suggesting that the dimeric form was more susceptible to the inhibition than the tetrameric form of the enzyme.Oxalate, ketomalonate, hydroxymalonate, malonate, oxaloacetate, tartrate, α-hydroxybutyrate, α-ketobutyrate, α-ketoglutarate and α-hydroxyglutarate exhibited linear competitive inhibition with respect to the substrate L-malate at pH 8.0. On the other hand, glyoxylate and glycolate turned out to be non-competitive inhibitors, while glycolaldehyde, succinate, fumarate, maleate and β- and γ-hydroxybutyrate had no effect on the enzyme activity, at the concentrations assayed. These results suggest that the extent of inhibition was dependent on the size of the analogues and that the presence of an 1-carboxyl group along with a 2-hydroxyl or 2-keto group was important for binding of the substrate analogue to the enzyme.

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Section: Resultscontrasting

confidence: 62%

Interaction of analogues of substrate with NADP-malic enzyme from maize leaves

1994

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“…An earlier report from Asami et al (1979a), pointed out that NADP-ME from maize leaf appears to be regulated by an interaction between pH, Mg 2÷ and L-malate as well as by the NADPH to NADP ÷ ratio. Although this and other works have shown regulation of NADP-ME from C 4 plants by different metabolites (Davies et al 1974, Asami et al 1979a, Iglesias and Andreo 1989, Ashton et al 1990, the characterization of the regulatory properties of the protein is far from complete.…”

Section: Introductionmentioning

confidence: 86%

Hysteretic properties of NADP-malic enzyme from sugarcane leaves

Iglesias

Andreo

1992

Photosynth Res

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NADP-malic enzyme highly purified from sugarcane leaves exhibited hysteretic properties. This behavior resulted in a lag phase during activity measurement of the enzyme preincubated in the absence of substrates. The lag was inversely proportional to the protein concentration during preincubation, which suggests that changes in the aggregational state of the enzyme are responsible for hysteresis. The pH conditions as well as the presence of different compounds in the preincubation medium modified the hysteretic properties of the enzyme. Mg(2+) eliminated the lag period and increased the enzyme activity by nearly 2-fold. NADP(+), 3-phosphoglycerate, ATP and dithiothreitol shortened the lag phase. The substrate L-malate inhibited the enzyme by decreasing the steady state velocity and increasing the lag time in a concentration-dependent manner. NADPH, triose-phosphates and high ionic strength increased the lag phase. Results are consistent with the view that the level of different metabolites and the pH conditions at the chloroplast regulate the activity of NADP-malic enzyme in a coordinate and effective manner.

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“…According to these authors, ME was present in flood susceptible species but absent in flood tolerant species. The results were later refuted by Davies et al (1974) who reported the wide distribution of ME in both flood tolerant and flood susceptible species. In our study, the seed quality, genotype, and flooding temperature showed no significant effects on ME activities determined in the sample extracts.…”

Section: Malic Enzyme Activity During Floodingmentioning

confidence: 94%

“…ADH was assayed using the method described by Lai and Scandalios (1982). LDH was assayed according to the method of Davies and Davies (1972) and ME was assayed by the procedure detailed by Davies et al, (1974). Duplicate samples were assayed from each of the four replications of each treatment.…”

Section: Protein Extraction and Enzyme Assaymentioning

confidence: 99%

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Anaerobic metabolism enzymes as markers of flooding stress in maize seeds

1987

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Maize (Zea mays L.) seeds differ in their relative tolerance to the anaerobic environment caused by flooding. Seed tolerance to flooding stress depends on cellular and metabolic processes since gross anatomical responses have not developed at the pre-emergence stage. The study reported here characterizes the activities of four anaerobic respiratory enzymes: pyruvate decarboxylase (PDC), alcohol dehydrogenase (ADH), lactate dehydrogenase (LDH), and malic enzyme (ME) in the flood-tolerant A632 and floodsusceptible Mo 17 inbred maize seeds during flooding at 10 and 25 ~ Each inbred consisted of two seed lots possessing 95 % and 75 % germination levels. Flooding increased the activities of all four enzymes. However, no consistent correlation between anaerobic enzyme activity and flood tolerance was observed across genotype, seed quality and flooding temperature. The results indicate that it may not be feasible to use whole-seed anaerobic enzyme activities to predict maize seed performance under flooding stress.

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The distribution and properties of NADP malic enzyme in flowering plants

Cited by 33 publications

References 10 publications

Interaction of analogues of substrate with NADP-malic enzyme from maize leaves

Interaction of analogues of substrate with NADP-malic enzyme from maize leaves

Hysteretic properties of NADP-malic enzyme from sugarcane leaves

Anaerobic metabolism enzymes as markers of flooding stress in maize seeds

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