malic enzyme/majs

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CO2 is the inorganic carbon substrate of NADP malic enzymes from Zea mays and from wheat germ.

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NADP malic enzyme (EC 1.1.1.40) was extracted and partially purified from the green leaves of Zea mays var. Felix and from wheat germ. The active inorganic carbon species for both enzymes was, in contrast to an earlier report, CO2 not HCO3-. The apparent Km, CO2 for the maize enzyme was 1.2 mM and

Basic residues play key roles in catalysis and NADP(+)-specificity in maize (Zea mays L.) photosynthetic NADP(+)-dependent malic enzyme.

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C(4)-specific (photosynthetic) NADP(+)-dependent malic enzyme (NADP(+)-ME) has evolved from C(3)-malic enzymes and represents a unique and specialized form, as indicated by its particular kinetic and regulatory properties. In the present paper, we have characterized maize (Zea mays L.)

Kinetics and functional diversity among the five members of the NADP-malic enzyme family from Zea mays, a C4 species.

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NADP-malic enzyme (NADP-ME) is involved in different metabolic pathways in several organisms due to the relevant physiological functions of the substrates and products of its reaction. In plants, it is one of the most important proteins that were recruited to fulfil key roles in C4 photosynthesis.

[Multiple molecular forms of "malic" enzyme from zea mays leaves].

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Using 7.5% polyacrylamide gel electrophoresis, a heterogeneity of molecular forms of "malic" enzyme (EC 1.1.1.40) in corn leaves was established. Etyolated corn sprouts contain only one component of the enzyme, while in the green leaves 3 minor components were additionally found. A possible

Association of NADP- and NAD-linked malic enzyme acitivities in Zea mays: relation to C4 pathway photosynthesis.

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A two-dimensional microscale model of gas exchange during photosynthesis in maize (Zea mays L.) leaves.

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CO2 exchange in leaves of maize (Zea mays L.) was examined using a microscale model of combined gas diffusion and C4 photosynthesis kinetics at the leaf tissue level. Based on a generalized scheme of photosynthesis in NADP-malic enzyme type C4 plants, the model accounted for CO2 diffusion in a leaf

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

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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

Regulation of the expression of NADP-malic enzyme by UV-B, red and far-red light in maize seedlings.

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The induction of nicotinamide adenine dinucleotide phosphate-malic enzyme (NADP-ME) in etiolated maize (Zea mays) seedlings by UV-B and UV-A radiation, and different levels of photosynthetically active radiation (PAR, 400-700 nm) was investigated by measuring changes in activity, protein quantity

Functional characterization of residues involved in redox modulation of maize photosynthetic NADP-malic enzyme activity.

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Two highly similar plastidic NADP-malic enzymes (NADP-MEs) are found in the C(4) species maize (Zea mays); one exclusively expressed in the bundle sheath cells (BSCs) and involved in C(4) photosynthesis (ZmC(4)-NADP-ME); and the other (ZmnonC(4)-NADP-ME) with housekeeping roles. In the present work,

Isolation of Bundle Sheath Cell Chloroplasts from the NADP-ME Type C(4) Plant Zea mays: Capacities for CO(2) Assimilation and Malate Decarboxylation.

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Bundle sheath chloroplasts have been isolated from Zea mays leaves by a procedure involving enzymic digestion of mechanically prepared strands of bundle sheath cells followed by gentle breakage and filtration. The resulting crude chloroplast preparation was enriched by Percoll density layer

Analogues of NADP(+) as inhibitors and coenzymes for NADP(+) malic enzyme from maize leaves.

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Structural analogues of the NADP(+) were studied as potential coenzymes and inhibitors for NADP(+) dependent malic enzyme from Zea mays L. leaves. Results showed that 1, N(6)-etheno-nicotinamide adenine dinucleotide phosphate (∈ NADP(+)), 3-acetylpyridine-adenine dinucleotide phosphate (APADP(+)),

Evidence for the Existence of Two Essential and Proximal Cysteinyl Residues in NADP-Malic Enzyme from Maize Leaves.

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Incubation of maize (Zea mays) leaf NADP-malic enzyme with monofunctional and bifunctional N-substituted maleimides results in an irreversible inactivation of the enzyme. Inactivation by the monofunctional reagents, N-ethylmaleimide (NEM) and N-phenylmaleimide, followed pseudo-first-order kinetics.

Isolation and characterization of cDNA clones for NADP-malic enzyme from leaves of Flaveria: transcript abundance distinguishes C3, C3-C4 and C4 photosynthetic types.

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To study the control of enhanced synthesis of enzymes associated with C4 photosynthesis relative to non-C4 plants, we investigated the expression of NADP-malic enzyme (NADP-ME) in different photosynthetic types of Flaveria. Complementary DNA clones encoding NADP-ME were constructed using poly(A)+

Light-stimulated synthesis of NADP malic enzyme in leaves of maize.

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Illumination of etiolated maize plants for 80 h brings about a 15-20-fold increase in activity of NADP malic enzyme (EC 1.1.1.40). Increases in NADP malic enzyme protein and in the level of translatable mRNA for this protein occur simultaneously with the activity increase. Radiolabeled amino acids

Contribution of malic enzyme, pyruvate kinase, phosphoenolpyruvate carboxylase, and the krebs cycle to respiration and biosynthesis and to intracellular pH regulation during hypoxia in maize root tips observed by nuclear magnetic resonance imaging and gas chromatography-mass spectrometry

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In vivo pyruvate synthesis by malic enzyme (ME) and pyruvate kinase and in vivo malate synthesis by phosphoenolpyruvate carboxylase and the Krebs cycle were measured by 13C incorporation from [1-13C]glucose into glucose-6-phosphate, alanine, glutamate, aspartate, and malate. These metabolites were

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