We revealed the functional characterization of C4-NADP-malic enzyme (NADP-ME), extracted and partially purified from maize (Zea maysL. cv. Kaveri 50). The leaf discs were previously activated under 1000–1200 µE m−2s−1, incubated in bicarbonate (2.0 mM) solution, and subjected to salt stress (100 mM NaCl). Initially, salt stress was evident from the accumulations of proline, chlorophyll content, carbohydrate profile, and Hill activity influencing the C4 enzyme. Primarily, in illuminated tissues, the activity of the enzyme recorded a reduced trend through salinity irrespective of light and darkness compared to the control. On illumination, the kinetic parameters such as Vmax of the enzyme increased by 1.36-fold compared to in the dark under salinity whereas Km was decreased by 20% under the same condition. The extent of light induction was proportionate to limiting (0.01 mM) and saturated (4.0 mM) malate concentrations for enzyme activity. Moreover, the catalytic properties of the enzyme were also tested on concomitant responses to activator (citrate and succinate) and inhibitor (oxalate and pyruvate) residues. The sensitivity to light and dark effects was also tested for reducing agents such as dithiothreitol, suggesting the effect of the changes in redox on the regulatory properties of the enzyme. The ratio of enzyme activity under light and darkness in the presence or absence of a reducing agent was concomitantly increased with varying malate concentrations. At the molecular level, protein polymorphism of the enzyme represented minor variations in band intensities, however, not in numbers through salinity subjected to light and darkness. Therefore, salinity-induced changes in the decarboxylation reaction, evident by NADP-ME activity, may be based on the redox property of regulatory sites and sensitivity to light and darkness.