Abstract
Three new nicotinamide adenine dinucleotide (NAD) analogs were synthesized, and their characteristics as cofactors for Escherichia coli malic enzyme (ME) and its double mutant ME L310R/Q401C were analyzed. Each pair of the NAD analog and the double mutant showed good orthogonality to the natural pair of NAD and ME in terms of catalyzing oxidative decarboxylation of l-malic acid. Results indicated that molecular interactions between redox enzyme and cofactor could be further explored to generate new bioorthogonal redox systems.
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