Catalyzes the decarboxylation of malate to pyruvate (PubMed:17557829). In vitro, shows malolactic enzyme activity in the presence of NADPH. However, it is unlikely that this activity is of relevance in E.coli, which produces little NADPH (PubMed:33824210). (S)-malate + NADP(+) = CO2 + NADPH + pyruvate H(+) + oxaloacetate = CO2 + pyruvate Divalent metal cations. Prefers magnesium or manganese. Inhibited by 4 mM Mg(2+) and acetyl-CoA, competitively inhibited by fumarate and oxaloacetate. Activated by glutamate and aspartate, glucose-6-phosphate, acetyl-phosphate and 2 mM KCl. Optimum pH is 7.5 for L-malate. Homooligomer, possibly an octamer. The-C-terminal phosphate acetyltransferase domain is responsible for oligomerization, and is responsible for inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate as shown by its deletion. The isolated domain does not catalyze the interconversion of acetyl-CoA and acetyl-phosphate. Cannot use NAD(+). In the N-terminal section; belongs to the malic enzymes family. In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.