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Hysteretic properties of NADP-malic enzyme from sugarcane leaves
Photosynthesis Research, 1992NADP-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 ...
A A, Iglesias, C S, Andreo
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Kinetic mechanism of NADP-malic enzyme from maize leaves
Photosynthesis Research, 1995The 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.
C P, Spampinato, C S, Andreo
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NADP-malic enzyme from maize leaf: Regulatory properties
Archives of Biochemistry and Biophysics, 1979The regulatory properties of purified maize leaf NADP-malic enzyme (EC 1.1.1.40) were studied at three different pHs and the following results were obtained. (a) At pH 7.5 enzyme activity reaches a maximum at 0.4–0.8 mm malate depending on the Mg2+ concentration, and higher levels of malate result in marked substrate inhibition; with increasing pH the ...
S, Asami, K, Inoue, T, Akazawa
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Review: The role of NADP-malic enzyme in plants under stress
Plant Science, 2019Under natural conditions, plants constantly encounter various fluctuating environmental stresses, which potentially restrict plant growth, plant development and even limit crop productivity. In addition to carbon fixation activity in C4 photosynthesis, NADP-dependent malic enzyme (NADP-ME) has been suggested to play important roles in diverse stress ...
Qiqi Chen +4 more
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Characterization of the NADP-malic enzymes in the woody plant Populus trichocarpa
Molecular Biology Reports, 2012Plant NADP-malic enzyme (NADP-ME, EC 1.1.1.40) participates in a large number of metabolic pathways, but little is known about the NADP-ME family in woody plants or trees. Here, we characterized the tree Populus trichocarpa NADP-ME (PtNADP-ME) family and the properties of the family members.
Qiguo, Yu +6 more
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NADP-malic enzyme from maize leaf: Purification and properties
Archives of Biochemistry and Biophysics, 1979Abstract NADP-malic enzyme (EC 1.1.1.40), which is involved in the photosynthetic C 4 pathway, was isolated from maize leaf and purified to apparent homogeneity as judged by polyacrylamide gel electrophoresis. At the final step, chromatography on Blue-Sepharose, the enzyme had been purified approximately 80-fold from the initial crude extract and ...
S, Asami +4 more
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The distribution and properties of NADP malic enzyme in flowering plants
Phytochemistry, 1974Abstract Malic enzyme is shown to be widely distributed in higher plants and contrary to earlier reports is present in the roots of flood tolerant species. Excluding members of the Gramineae, the malic enzyme from 27 out of 28 species examined was shown to exhibit allosteric properties.
D.D. Davies, K.H. Nascimento, K.D. Patil
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Malate metabolism by NADP-malic enzyme in plant defense
Photosynthesis Research, 1999Malate is involved in various metabolic pathways, and there are several enzymes that metabolize it. One important malate metabolizing enzyme is NADP-malic enzyme (NADP-ME). NADP-ME functions in many different pathways in plants, having an important role in C4 photosynthesis where it releases the CO2 to be used in carbon fixation by Rubisco.
Paula Casati +3 more
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Hysteresis of cytosolic NADP-malic enzyme II from Trypanosoma cruzi
Molecular and Biochemical Parasitology, 1994NADP-malic enzyme II, one of two isoenzymes of NADP-malic enzyme (EC 1.1.1.40) in Trypanosoma cruzi epimastigotes, presents hysteretic behavior that results in a kinetic lag in the reaction progress curve. The lag is affected by the malate, aspartate and oxaloacetate concentrations in the assay mixture.
L, Avilán, P, García
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Interaction of analogues of substrate with NADP-malic enzyme from maize leaves
Photosynthesis Research, 1994The 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 ...
C P, Spampinato +2 more
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