Results 181 to 190 of about 10,930 (224)

Properties of NADP-malic enzyme from glumes of developing wheat grains

Phytochemistry, 1985
Abstract Properties of partially purified NADP-malic enzyme (EC 1.1.1.40) from glumes of developing wheat grains were examined. The pH optimum for enzyme activity was influenced by malate and shifted from 7.3 to 7.6 when the concentration of malate was increased from 2 to 10 mM.
Santosh Dhillon, S.K. Suneja, S.K. Sawhney, R. Singh   +3 more
exaly   +3 more sources

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NADP-malic enzyme from plants

Phytochemistry, 1992
NADP-malic enzyme functions in plant metabolism as a decarboxylase of malate in the chloroplast or cytosol. It serves as a source of CO2 for photosynthesis in the bundle sheath chloroplasts of C4 plants and in the cytosol of Crassulacean acid metabolism plants, and as a source of NADPH and pyruvate in the cytosol of various tissues.
Edwards Gerald E, Andreo CARLOS S, G E Edwards   +2 more
exaly   +3 more sources

NADP–Malic Enzyme from the C4PlantFlaveria bidentis:Nucleotide Substrate Specificity

Archives of Biochemistry and Biophysics, 1997
NADP-malic enzyme (NADP-ME, EC 1.1.1.40) was purified to near-homogeneity from leaves of the C4 dicot Flaveria bidentis and shown to possess intrinsic NAD-dependent malic enzyme activity. The NAD-dependent activity is optimal at pH 7.5 and in the presence of Mn2+.
Anthony R Ashton
exaly   +3 more sources

Molecular adaptations of NADP-malic enzyme for its function in C4 photosynthesis in grasses

Nature Plants, 2019
In C4 grasses of agronomical interest, malate shuttled into the bundle sheath cells is decarboxylated mainly by nicotinamide adenine dinucleotide phosphate (NADP)-malic enzyme (C4-NADP-ME). The activity of C4-NADP-ME was optimized by natural selection to efficiently deliver CO2 to Rubisco.
Clarisa E. Alvarez, Anastasiia Bovdilova, Astrid Höppner, Christian-Claus Wolff, Mariana Saigo, Felipe Trajtenberg, Tao Zhang, Alejandro Buschiazzo, Luitgard Nagel-Steger, Maria F. Drincovich, Martin J. Lercher, Veronica G. Maurino   +11 more
openaire   +6 more sources

Primary structure of NADP-dependent malic enzyme in the dicotyledonous C4plantFlaveria trinervia

FEBS Letters, 1990
The primary structure of NADP-dependent malic enzyme (NADP-ME) of the dicotyledonous C4 plant Flaveria trinervia was determined from sequence analysis of a cDNA clone containing the complete coding region. Comparison of the mature F.
Peter Westhoff
exaly   +2 more sources

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

International Journal of Molecular Sciences, 2009
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.
Karel Müller, Noémi Čeřovská, Helena Synkova   +2 more
exaly   +2 more sources

Evidence for a cytosolic NADP-malic enzyme in tomato

Phytochemistry, 1996
Abstract The similarity and cellular location of NADP + -malic enzyme (NADP-ME, EC 1.1.1.40) in developing fruit and other parts of the tomato ( Lycopersicon esculentum Mill.) plant were investigated in order to clarify the role of the enzyme in metabolism.
Michael Knee, Fernando L. Finger, L. Mark Lagrimini   +2 more
openaire   +1 more source

The Enzyme Kinetics of the NADP-Malic Enzyme from Tobacco Leaves

Collection of Czechoslovak Chemical Communications, 2007
Malic enzyme (L-malate: NADP+ oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40, NADP-ME), which was found in chloroplasts, was isolated from tobacco leaves (Nicotiana tabacum L.) almost homogenous. The specific enzyme activity was 0.95 μmol min-1 mg-1. The enzyme pH optimum was found between pH 7.1 and 7.4.
Helena Ryšlavá, Veronika Doubnerová, Karel Muller, Petra Baťková, Renáta Schnablová, Jiří Liberda, Helena Synková, Noemi Čeřovská   +7 more
openaire   +1 more source

Hysteretic properties of NADP-malic enzyme from sugarcane leaves

Photosynthesis Research, 1992
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 ...
A A, Iglesias, C S, Andreo
openaire   +2 more sources

NADP-malic enzyme from maize leaf: Regulatory properties

Archives of Biochemistry and Biophysics, 1979
The 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
openaire   +2 more sources