Isolation and characterization of cytoplasmic NADP<sup>+</sup>‐malic enzyme from <i>Lupinus luteus</i> leaves

Tomaszewska, Barbara; Schramm, Ryszard W.; Kokot, Anna; Mazurowa, H.

doi:10.1111/j.1399-3054.1983.tb06293.x

Cited by 8 publications

(3 citation statements)

References 18 publications

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“…The apparent K,, values for NADP* and L-malate were 31 |iM and 4.0 mM, respectively. Tbe K^ value for NADP* is in good agreement with that reported for the enzyme from leaves of maize (Johnson and Hatch 1970, Ziegler 1974, Asami et al 1979, Lupinus tuteus (Tomaszewska et al 1983), mango pulp (Krisbnamurthy and Patwardhan 1971) and wheat glumes (Dhillon et al 1985). However, K^ for malate of tbe enzyme from pod walls of chickpea was substantially higher than that from other plants.…”

Section: Effect Of Substratessupporting

confidence: 87%

“…Its effect was non-competitive against malate and its estimated K; value was 0.55 mM. Marked inbibition of NADP*-malic enzyme by oxalate has been reported earlier (Bhagwat et al 1977, Tomaszewska et al, 1983, Dhillon et al 1985, but the inhibitory mechanism bas not been described. Sodium oxaloacetate at 2.5 mM diminished the enzyme activity by 50% and its K| value was 0.79 mM.…”

Section: Effect Of Organic Acidsmentioning

confidence: 83%

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Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Das

Sood

Sawhney

et al. 1986

Physiologia Plantarum

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NADP+‐malic enzyme (l‐malate: NADP+ oxidoreductase, decarboxylating EC 1.1.1.40) from pod walls of chickpea was purified 51‐fold by ammonium sulphate fractionation, DEAE‐ cellulose chromatography and gel filtration through Sepharose 4B. The purified enzyme required a divalent cation, either Mn2+ or Mg2+, for its activity. Km values at pH 7.8 for malate, NADP+ and Mn2+ were 4.0, 0.031 and 0.71 mM, respectively. Mn2+‐dependent activity was inhibited by heavy metal ions such as Cd2+, Zn2+, Hg2+, and to a lesser extent by Pb2+ and Al3+. Among the organic acids examined, sodium salts of oxalate and oxaloacetate were inhibitory. Kinetics of the reaction mechanism showed sequential binding of malate and NADP+ to the enzyme. Products of reaction, viz. pyruvate, bicarbonate and NADPH, inhibited the enzyme activity. At limiting concentrations of NADP+, pyruvate and bicarbonate induced a positive cooperative effect by malate. It is proposed that the activity of NADP+‐malic enzyme is controlled by intracellular concentrations of substrates and products.

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Section: Effect Of Substratessupporting

confidence: 87%

Section: Effect Of Organic Acidsmentioning

confidence: 83%

Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Das

Sood

Sawhney

et al. 1986

Physiologia Plantarum

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“…In Bryophyllum calycinum and Crassula lycopodioides (24) and in Mesembryanthemum crystallinum (30), it was reported mostly or totally in the cytosol. In C3 plants NADP:malic enzyme was restricted to the cytosol (8,27).…”

mentioning

confidence: 99%

Purification by Immunoadsorption and Immunochemical Properties of NADP-Dependent Malic Enzymes from Leaves of C₃, C₄, and Crassulacean Acid Metabolism Plants

Fathi

Schnarrenberger²

1990

Plant Physiol.

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NADP:malic enzyme from com (Zea mays L.) leaves was purified by conventional techniques to apparent homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Antibodies raised against this protein in rabbits were purified, coupled covalently to protein A-Sepharose CL-4B, and used as an immunoaffinity resin to purify the NADP:malic enzymes of the C3 plants spinach (Spinacia oleracea L.) and wheat (Triticum aestivum L.), of the Crassulacean acid metabolism (CAM) plant Bryophyllum daigremontianum R. Hamed et Perr. de la Bathie and the C4 plants corn, sugarcane (Saccharum officinarum L.), and Portulaca grandHflora L. Such procedures yielded homogeneous protein preparations with a single protein band, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, except for P. grandiflora L. with two bands. The specific activities of the purified proteins ranged between 56 and 91 units (milligrams per protein). NADP:malic enzyme represented up to 1% of the total soluble protein in C4 plants, 0.5% in the CAM plant, and less than 0.01% in C3 plants. In immunotitration tests involving immunoprecipitation and immunoinhibition of activity by an antiserum against the corn leaf enzyme, the NADP:malic enzymes of com and sugarcane shQwed virtually full identity of epitopes, while the NADP:malic enzymes of the C3 and CAM plants exhibited a cross-reaction of one-twentieth and one-fourth by these tests, respectively. The NADP:malic enzyme of P. grandlflora exhibited characteristics more closely related to the enzymes of C3 and CAM plants than to those of C4 plants.

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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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Isolation and characterization of cytoplasmic NADP⁺‐malic enzyme from Lupinus luteus leaves

Cited by 8 publications

References 18 publications

Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Purification by Immunoadsorption and Immunochemical Properties of NADP-Dependent Malic Enzymes from Leaves of C₃, C₄, and Crassulacean Acid Metabolism Plants

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

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Isolation and characterization of cytoplasmic NADP+‐malic enzyme from Lupinus luteus leaves

Cited by 8 publications

References 18 publications

Properties of NADP+‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Properties of NADP+‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Purification by Immunoadsorption and Immunochemical Properties of NADP-Dependent Malic Enzymes from Leaves of C3, C4, and Crassulacean Acid Metabolism Plants

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

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Isolation and characterization of cytoplasmic NADP⁺‐malic enzyme from Lupinus luteus leaves

Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Properties of NADP⁺‐malic enzyme from pod walls of chickpea (Cicer arietinum)

Purification by Immunoadsorption and Immunochemical Properties of NADP-Dependent Malic Enzymes from Leaves of C₃, C₄, and Crassulacean Acid Metabolism Plants