Identification of malic enzyme mutants depending on 1,2,3-triazole moiety-containing nicotinamide adenine dinucleotide analogs
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Updated: May 3, 2026
A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1
Published on: April 16, 2021
Shuhua Hou1, Debin Ji2, Wujun Liu2
1Division of Biotechnology and State Key Laboratory of Catalysis, Dalian Institute of Chemical Physics, CAS, Dalian 116023, China; Department of Chemistry, Liaoning Key Laboratory for the Synthesis and Application of Functional Compounds, Bohai University, Jinzhou 121013, China.
Abstract:
An activity screening between 1,2,3-triazole moiety-containing nicotinamide adenine dinucleotide (NAD) analogs and malic enzyme (ME) mutants identified some mutants capable of taking NAD analogs as the cofactor. One particular pair, ME-L310K/L404S and the analog B-8 had good catalytic efficiency and cofactor specificity. The new system gained about 1200-fold cofactor specificity shift from NAD toward B-8 in terms of oxidative decarboxylation of l-malate. Our results provided insightful information for the development of orthogonal redox system that is of particular important to precisely control engineered metabolic pathways.
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