The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It exhibits a strict enantioselectivity and accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.422, pseudoephedrine dehydrogenase and EC 1.5.1.18, ephedrine dehydrogenase.
History
EC 1.1.1.423 created 2020, modified 2020
Reference
1
Authors
Shanati, T., Lockie, C., Beloti, L., Grogan, G. and Ansorge-Schumacher, M.B.
Title
Two enantiocomplementary ephedrine dehydrogenases from Arthrobacter sp. TS-15 with broad substrate specificity.
Journal
ACS Catal 9:6202-6211 (2019)
Reference
2
Authors
Shanati, T., Ansorge-Schumacher, M.
Title
Enzymes and methods for the stereoselective reduction of carbonyl compounds, oxidation and stereoselective reductive amination - for the enantioselective preparation of alcohol amine compounds.
