作者: Bettina R. Bommarius , Martin Schürmann , Andreas S. Bommarius
DOI: 10.1039/C4CC06527A
关键词: Substrate specificity 、 Acetophenone 、 Chemistry 、 Phenylalanine 、 Biochemistry 、 Enzyme 、 Amine dehydrogenase 、 Amination 、 Turn (biochemistry) 、 Leucine
摘要: 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 phenylalanine DH, respectively. Unlike the proteins, AmDH (‘cFL-AmDH’) catalyzes amination acetophenone to (R)-methylbenzylamine adamantylmethylketone adamantylethylamine.