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A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant <i>Thermococcus kodakarensis</i> has an altered cofactor preference for NAD⁺, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from <i>Sulfolobus solfataricus</i> and NAD⁺/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.