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A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes
102
Citations
10
References
2014
Year
BiosynthesisEngineeringAldehyde DehydrogenaseBiochemistryAldo-keto ReductaseNatural SciencesBiocatalysisSubstrate SpecificityMolecular BiologyEnzyme SpecificityOrganic ChemistryParent AmdhsEnzymatic ModificationDomain ShufflingAlcohol DehydrogenasesChimeric AmdhParent Enzymes
We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs ('L- and F-AmDH'), which in turn had been generated from leucine and phenylalanine DH, respectively. Unlike the parent proteins, the chimeric AmDH ('cFL-AmDH') catalyzes the amination of acetophenone to (R)-methylbenzylamine and adamantylmethylketone to adamantylethylamine.
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